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Dihydropyrimidine dehydrogenase [NADP(+)]

Intermolecular
Cysteine 82 and cysteine 956
Cysteine 82 and cysteine 953
Intramolecular
Cysteine 49 and cysteine 52
Cysteine 322 and cysteine 324
Cysteine 996 and cysteine 1001
Cysteine 126 and cysteine 130
Cysteine 130 and cysteine 136
Cysteine 671 and cysteine 684
Cysteine 956 and cysteine 996
Cysteine 953 and cysteine 959
More...
Cysteine 79 and cysteine 140
Cysteine 79 and cysteine 87
Cysteine 986 and cysteine 989
Cysteine 953 and cysteine 1001
Cysteine 986 and cysteine 992
Cysteine 953 and cysteine 996
Cysteine 91 and cysteine 130
Cysteine 963 and cysteine 986
Cysteine 79 and cysteine 82
Cysteine 82 and cysteine 140
Cysteine 959 and cysteine 996
Cysteine 87 and cysteine 140
Cysteine 91 and cysteine 136
Cysteine 963 and cysteine 989
Cysteine 953 and cysteine 956
Cysteine 963 and cysteine 992
Cysteine 956 and cysteine 959
Cysteine 82 and cysteine 87
Cysteine 989 and cysteine 992
Cysteine 257 and cysteine 322
Cysteine 992 and cysteine 996
Cysteine 643 and cysteine 671
Cysteine 52 and cysteine 385
Cysteine 91 and cysteine 126
Cysteine 87 and cysteine 136
Cysteine 87 and cysteine 91
Cysteine 959 and cysteine 992
Cysteine 136 and cysteine 140
Cysteine 956 and cysteine 1001
Cysteine 643 and cysteine 684
A redox-regulated disulphide may form between two units of Dihydropyrimidine dehydrogenase [NADP(+)] at cysteines 82 and 956. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide A name
Dihydropyrimidine dehydrogenase [NADP(+)]
Peptide B name
Dihydropyrimidine dehydrogenase [NADP(+)]
Peptide A accession
Q28943
Peptide B accession
Q28943
Peptide A residue number
82
Peptide B residue number
956

Ligandability

Cysteine 82 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 956 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Dihydropyrimidine dehydrogenase [NADP(+)] at cysteines 82 and 953. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide A name
Dihydropyrimidine dehydrogenase [NADP(+)]
Peptide B name
Dihydropyrimidine dehydrogenase [NADP(+)]
Peptide A accession
Q28943
Peptide B accession
Q28943
Peptide A residue number
82
Peptide B residue number
953

Ligandability

Cysteine 82 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 953 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 49 and 52.

Details

Redox score ?
81
PDB code
1h7w
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig
Structure deposition date
2001-01-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
42
Peptide accession
Q28943
Residue number A
49
Residue number B
52
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 49 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 52 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 322 and 324.

Details

Redox score ?
79
PDB code
1gte
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, binary complex with 5- iodouracil
Structure deposition date
2002-01-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
8
Peptide accession
Q28943
Residue number A
322
Residue number B
324
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 322 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 324 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 996 and 1001.

Details

Redox score ?
67
PDB code
1gt8
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and uracil-4-acetic acid
Structure deposition date
2002-01-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
100
Peptide accession
Q28943
Residue number A
996
Residue number B
1001
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 996 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1001 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 126 and 130.

Details

Redox score ?
64
PDB code
8f5w
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine and nadph quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
Q28943
Residue number A
126
Residue number B
130
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 126 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 130 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 130 and 136.

Details

Redox score ?
61
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
14
% buried
nan
Peptide accession
Q28943
Residue number A
130
Residue number B
136
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 130 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 136 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 671 and 684. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
1gt8
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and uracil-4-acetic acid
Structure deposition date
2002-01-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
60
Peptide accession
Q28943
Residue number A
671
Residue number B
684
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 671 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 684 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 956 and 996. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7ljs
Structure name
porcine dihydropyrimidine dehydrogenase (dpd) complexed with 5- ethynyluracil (5eu) - open form
Structure deposition date
2021-01-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
100
Peptide accession
Q28943
Residue number A
956
Residue number B
996
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 956 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 996 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 953 and 959. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
Q28943
Residue number A
953
Residue number B
959
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 953 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 959 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 79 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
Q28943
Residue number A
79
Residue number B
140
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 79 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 140 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 79 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
Q28943
Residue number A
79
Residue number B
87
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 79 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 87 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 986 and 989. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
93
Peptide accession
Q28943
Residue number A
986
Residue number B
989
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 986 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 989 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 953 and 1001. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7lju
Structure name
porcine dihydropyrimidine dehydrogenase (dpd) crosslinked with 5- ethynyluracil (5eu)
Structure deposition date
2021-01-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
100
Peptide accession
Q28943
Residue number A
953
Residue number B
1001
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 953 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1001 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 986 and 992. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8f5w
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine and nadph quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
93
Peptide accession
Q28943
Residue number A
986
Residue number B
992
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 986 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 992 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 953 and 996. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1gte
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, binary complex with 5- iodouracil
Structure deposition date
2002-01-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
100
Peptide accession
Q28943
Residue number A
953
Residue number B
996
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 953 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 996 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 91 and 130. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide accession
Q28943
Residue number A
91
Residue number B
130
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 91 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 130 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 963 and 986. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
10
% buried
94
Peptide accession
Q28943
Residue number A
963
Residue number B
986
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 963 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 986 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 79 and 82. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
1gth
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and 5-iodouracil
Structure deposition date
2002-01-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide accession
Q28943
Residue number A
79
Residue number B
82
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 79 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 82 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 82 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
100
Peptide accession
Q28943
Residue number A
82
Residue number B
140
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 82 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 140 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 959 and 996. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1gth
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and 5-iodouracil
Structure deposition date
2002-01-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
Q28943
Residue number A
959
Residue number B
996
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 959 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 996 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 87 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7ljs
Structure name
porcine dihydropyrimidine dehydrogenase (dpd) complexed with 5- ethynyluracil (5eu) - open form
Structure deposition date
2021-01-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide accession
Q28943
Residue number A
87
Residue number B
140
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 87 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 140 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 91 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1gte
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, binary complex with 5- iodouracil
Structure deposition date
2002-01-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
95
Minimum pKa ?
10
% buried
100
Peptide accession
Q28943
Residue number A
91
Residue number B
136
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 91 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 136 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 963 and 989. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
100
Peptide accession
Q28943
Residue number A
963
Residue number B
989
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 963 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 989 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 953 and 956. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7ljs
Structure name
porcine dihydropyrimidine dehydrogenase (dpd) complexed with 5- ethynyluracil (5eu) - open form
Structure deposition date
2021-01-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
Q28943
Residue number A
953
Residue number B
956
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 953 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 956 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 963 and 992. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
103
Minimum pKa ?
12
% buried
100
Peptide accession
Q28943
Residue number A
963
Residue number B
992
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 963 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 992 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 956 and 959. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
Q28943
Residue number A
956
Residue number B
959
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 956 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 959 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 82 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
Q28943
Residue number A
82
Residue number B
87
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 82 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 87 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 989 and 992. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
8f6n
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with thymine quasi-anaerobically
Structure deposition date
2022-11-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
Q28943
Residue number A
989
Residue number B
992
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 989 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 992 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 257 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1gt8
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and uracil-4-acetic acid
Structure deposition date
2002-01-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
11
% buried
34
Peptide accession
Q28943
Residue number A
257
Residue number B
322
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 257 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 322 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 992 and 996. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
8
% buried
100
Peptide accession
Q28943
Residue number A
992
Residue number B
996
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 992 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 996 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 643 and 671. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1h7w
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig
Structure deposition date
2001-01-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
67
Peptide accession
Q28943
Residue number A
643
Residue number B
671
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 643 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 671 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 52 and 385. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1gt8
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and uracil-4-acetic acid
Structure deposition date
2002-01-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
86
Peptide accession
Q28943
Residue number A
52
Residue number B
385
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 52 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 385 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 91 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1gt8
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and uracil-4-acetic acid
Structure deposition date
2002-01-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
Q28943
Residue number A
91
Residue number B
126
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 91 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 126 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 87 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1h7x
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex of a mutant enzyme (c671a), nadph and 5-fluorouracil
Structure deposition date
2001-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
14
% buried
100
Peptide accession
Q28943
Residue number A
87
Residue number B
136
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 87 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 136 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 87 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7ljs
Structure name
porcine dihydropyrimidine dehydrogenase (dpd) complexed with 5- ethynyluracil (5eu) - open form
Structure deposition date
2021-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
8
% buried
100
Peptide accession
Q28943
Residue number A
87
Residue number B
91
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 87 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 91 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 959 and 992. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1gth
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and 5-iodouracil
Structure deposition date
2002-01-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
105
Minimum pKa ?
15
% buried
100
Peptide accession
Q28943
Residue number A
959
Residue number B
992
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 959 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 992 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 136 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
7ljs
Structure name
porcine dihydropyrimidine dehydrogenase (dpd) complexed with 5- ethynyluracil (5eu) - open form
Structure deposition date
2021-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
10
% buried
100
Peptide accession
Q28943
Residue number A
136
Residue number B
140
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 136 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 140 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 956 and 1001. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1gt8
Structure name
dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with nadph and uracil-4-acetic acid
Structure deposition date
2002-01-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide accession
Q28943
Residue number A
956
Residue number B
1001
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 956 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1001 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydropyrimidine dehydrogenase [NADP(+)] between cysteines 643 and 684. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
8f61
Structure name
dihydropyrimidine dehydrogenase (dpd) c671s mutant soaked with dihydrothymine quasi-anaerobically
Structure deposition date
2022-11-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
79
Peptide accession
Q28943
Residue number A
643
Residue number B
684
Peptide name
Dihydropyrimidine dehydrogenase [NADP(+)]

Ligandability

Cysteine 643 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 684 of Dihydropyrimidine dehydrogenase [NADP(+)]

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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