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a tool for identifying drug-targetable redox-active disulphides

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Xanthine dehydrogenase/oxidase

Intermolecular
Cysteine 487 and cysteine 1317
Cysteine 78 and cysteine 280
Intramolecular
Cysteine 536 and cysteine 993
Cysteine 594 and cysteine 749
Cysteine 43 and cysteine 48
Cysteine 51 and cysteine 73
Cysteine 116 and cysteine 148
Cysteine 1167 and cysteine 1310
Cysteine 113 and cysteine 150
Cysteine 509 and cysteine 1318
More...
Cysteine 43 and cysteine 73
Cysteine 972 and cysteine 1160
Cysteine 148 and cysteine 150
Cysteine 112 and cysteine 147
Cysteine 48 and cysteine 51
Cysteine 48 and cysteine 73
Cysteine 968 and cysteine 1248
Cysteine 116 and cysteine 150
Cysteine 487 and cysteine 1318
Cysteine 749 and cysteine 826
Cysteine 992 and cysteine 1166
Cysteine 1000 and cysteine 1160
Cysteine 1317 and cysteine 1325
Cysteine 968 and cysteine 972
Cysteine 436 and cysteine 455
Cysteine 78 and cysteine 280
Cysteine 593 and cysteine 825
Cysteine 43 and cysteine 51
Cysteine 112 and cysteine 115
Cysteine 487 and cysteine 509
Cysteine 889 and cysteine 968
Cysteine 536 and cysteine 1167
Cysteine 48 and cysteine 115
A redox-regulated disulphide may form between two units of Xanthine dehydrogenase/oxidase at cysteines 487 and 1317.

Details

Redox score ?
69
PDB code
3etr
Structure name
crystal structure of xanthine oxidase in complex with lumazine
Structure deposition date
2008-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Xanthine dehydrogenase/oxidase
Peptide B name
Xanthine dehydrogenase/oxidase
Peptide A accession
P80457
Peptide B accession
P80457
Peptide A residue number
487
Peptide B residue number
1317

Ligandability

Cysteine 487 of Xanthine dehydrogenase/oxidase

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 1317 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase at cysteines 78 and 280. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3nvv
Structure name
crystal structure of bovine xanthine oxidase in complex with arsenite
Structure deposition date
2010-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide A name
Xanthine dehydrogenase/oxidase
Peptide B name
Xanthine dehydrogenase/oxidase
Peptide A accession
P80457
Peptide B accession
P80457
Peptide A residue number
78
Peptide B residue number
280

Ligandability

Cysteine 78 of Xanthine dehydrogenase/oxidase

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 280 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 536 and 993.

Details

Redox score ?
83
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
536
Residue number B
993
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 536 of Xanthine dehydrogenase/oxidase

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 993 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 594 and 749.

Details

Redox score ?
72
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
594
Residue number B
749
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 594 of Xanthine dehydrogenase/oxidase

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 749 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 43 and 48.

Details

Redox score ?
72
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
86
Minimum pKa ?
7
% buried
100
Peptide accession
P47989
Residue number A
43
Residue number B
48
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 43 of Xanthine dehydrogenase/oxidase

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 48 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 51 and 73.

Details

Redox score ?
71
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
100
Peptide accession
P47989
Residue number A
51
Residue number B
73
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 51 of Xanthine dehydrogenase/oxidase

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 73 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 116 and 148.

Details

Redox score ?
68
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
P47989
Residue number A
116
Residue number B
148
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 116 of Xanthine dehydrogenase/oxidase

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 148 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 1167 and 1310.

Details

Redox score ?
68
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
1167
Residue number B
1310
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 1167 of Xanthine dehydrogenase/oxidase

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 1310 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 113 and 150.

Details

Redox score ?
68
PDB code
3eub
Structure name
crystal structure of desulfo-xanthine oxidase with xanthine
Structure deposition date
2008-10-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
113
Residue number B
150
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 113 of Xanthine dehydrogenase/oxidase

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 150 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 509 and 1318.

Details

Redox score ?
64
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
509
Residue number B
1318
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 509 of Xanthine dehydrogenase/oxidase

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 1318 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 43 and 73.

Details

Redox score ?
61
PDB code
3b9j
Structure name
structure of xanthine oxidase with 2-hydroxy-6-methylpurine
Structure deposition date
2007-11-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
43
Residue number B
73
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 43 of Xanthine dehydrogenase/oxidase

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 73 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 972 and 1160.

Details

Redox score ?
61
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
972
Residue number B
1160
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 972 of Xanthine dehydrogenase/oxidase

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 1160 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 148 and 150.

Details

Redox score ?
60
PDB code
3eub
Structure name
crystal structure of desulfo-xanthine oxidase with xanthine
Structure deposition date
2008-10-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
148
Residue number B
150
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 148 of Xanthine dehydrogenase/oxidase

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 150 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 112 and 147. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1wyg
Structure name
crystal structure of a rat xanthine dehydrogenase triple mutant (c535a, c992r and c1324s)
Structure deposition date
2005-02-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
96
Minimum pKa ?
7
% buried
100
Peptide accession
P22985
Residue number A
112
Residue number B
147
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 112 of Xanthine dehydrogenase/oxidase

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 147 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 48 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
96
Minimum pKa ?
7
% buried
100
Peptide accession
P47989
Residue number A
48
Residue number B
51
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 48 of Xanthine dehydrogenase/oxidase

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 51 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 48 and 73. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1n5x
Structure name
xanthine dehydrogenase from bovine milk with inhibitor tei-6720 bound
Structure deposition date
2002-11-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
48
Residue number B
73
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 48 of Xanthine dehydrogenase/oxidase

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 73 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 968 and 1248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
76
Peptide accession
P47989
Residue number A
968
Residue number B
1248
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 968 of Xanthine dehydrogenase/oxidase

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 1248 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 116 and 150. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
102
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
116
Residue number B
150
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 116 of Xanthine dehydrogenase/oxidase

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 150 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 487 and 1318. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
487
Residue number B
1318
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 487 of Xanthine dehydrogenase/oxidase

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 1318 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 749 and 826. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide accession
P47989
Residue number A
749
Residue number B
826
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 749 of Xanthine dehydrogenase/oxidase

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 826 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 992 and 1166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3b9j
Structure name
structure of xanthine oxidase with 2-hydroxy-6-methylpurine
Structure deposition date
2007-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
992
Residue number B
1166
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 992 of Xanthine dehydrogenase/oxidase

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 1166 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 1000 and 1160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
1000
Residue number B
1160
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 1000 of Xanthine dehydrogenase/oxidase

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 1160 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 1317 and 1325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3b9j
Structure name
structure of xanthine oxidase with 2-hydroxy-6-methylpurine
Structure deposition date
2007-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
1317
Residue number B
1325
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 1317 of Xanthine dehydrogenase/oxidase

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 1325 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 968 and 972. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
13
% buried
96
Peptide accession
P47989
Residue number A
968
Residue number B
972
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 968 of Xanthine dehydrogenase/oxidase

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 972 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 436 and 455. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3uni
Structure name
crystal structure of bovine milk xanthine dehydrogenase with nadh bound
Structure deposition date
2011-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80457
Residue number A
436
Residue number B
455
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 436 of Xanthine dehydrogenase/oxidase

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 455 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 78 and 280. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2e1q
Structure name
crystal structure of human xanthine oxidoreductase mutant, glu803val
Structure deposition date
2006-10-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47989
Residue number A
78
Residue number B
280
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 78 of Xanthine dehydrogenase/oxidase

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 280 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 593 and 825. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3an1
Structure name
crystal structure of rat d428a mutant, urate bound form
Structure deposition date
2010-08-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
100
Peptide accession
P22985
Residue number A
593
Residue number B
825
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 593 of Xanthine dehydrogenase/oxidase

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 825 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 43 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
19
% buried
100
Peptide accession
P47989
Residue number A
43
Residue number B
51
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 43 of Xanthine dehydrogenase/oxidase

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 51 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 112 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6a7x
Structure name
rat xanthine oxidoreductase, d428a variant, nad bound form
Structure deposition date
2018-07-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
99
Minimum pKa ?
18
% buried
100
Peptide accession
P22985
Residue number A
112
Residue number B
115
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 112 of Xanthine dehydrogenase/oxidase

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 115 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 487 and 509. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
nan
Peptide accession
P47989
Residue number A
487
Residue number B
509
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 487 of Xanthine dehydrogenase/oxidase

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 509 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 889 and 968. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
P47989
Residue number A
889
Residue number B
968
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 889 of Xanthine dehydrogenase/oxidase

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 968 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 536 and 1167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
2ckj
Structure name
human milk xanthine oxidoreductase
Structure deposition date
2006-04-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
17
% buried
nan
Peptide accession
P47989
Residue number A
536
Residue number B
1167
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 536 of Xanthine dehydrogenase/oxidase

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 1167 of Xanthine dehydrogenase/oxidase

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 Xanthine dehydrogenase/oxidase between cysteines 48 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
16
PDB code
1wyg
Structure name
crystal structure of a rat xanthine dehydrogenase triple mutant (c535a, c992r and c1324s)
Structure deposition date
2005-02-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
102
Minimum pKa ?
17
% buried
100
Peptide accession
P22985
Residue number A
48
Residue number B
115
Peptide name
Xanthine dehydrogenase/oxidase

Ligandability

Cysteine 48 of Xanthine dehydrogenase/oxidase

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 115 of Xanthine dehydrogenase/oxidase

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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