ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dihydropyrimidinase-related protein 3

Intramolecular
Cysteine 133 and cysteine 448
Cysteine 132 and cysteine 133
Cysteine 132 and cysteine 448
Cysteine 187 and cysteine 248
A redox-regulated disulphide may form within Dihydropyrimidinase-related protein 3 between cysteines 133 and 448. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4cnu
Structure name
crystal structure of wt human crmp-4 from lattice translocation
Structure deposition date
2014-01-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
104
Minimum pKa ?
13
% buried
100
Peptide accession
Q14195
Residue number A
133
Residue number B
448
Peptide name
Dihydropyrimidinase-related protein 3

Ligandability

Cysteine 133 of Dihydropyrimidinase-related protein 3

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 448 of Dihydropyrimidinase-related protein 3

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 Dihydropyrimidinase-related protein 3 between cysteines 132 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4cnu
Structure name
crystal structure of wt human crmp-4 from lattice translocation
Structure deposition date
2014-01-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
83
Peptide accession
Q14195
Residue number A
132
Residue number B
133
Peptide name
Dihydropyrimidinase-related protein 3

Ligandability

Cysteine 132 of Dihydropyrimidinase-related protein 3

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 133 of Dihydropyrimidinase-related protein 3

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 Dihydropyrimidinase-related protein 3 between cysteines 132 and 448. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4bkn
Structure name
human dihydropyrimidinase-related protein 3 (dpysl3)
Structure deposition date
2013-04-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
84
Peptide accession
Q14195
Residue number A
132
Residue number B
448
Peptide name
Dihydropyrimidinase-related protein 3

Ligandability

Cysteine 132 of Dihydropyrimidinase-related protein 3

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 448 of Dihydropyrimidinase-related protein 3

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 Dihydropyrimidinase-related protein 3 between cysteines 187 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4cnu
Structure name
crystal structure of wt human crmp-4 from lattice translocation
Structure deposition date
2014-01-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
82
Peptide accession
Q14195
Residue number A
187
Residue number B
248
Peptide name
Dihydropyrimidinase-related protein 3

Ligandability

Cysteine 187 of Dihydropyrimidinase-related protein 3

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 248 of Dihydropyrimidinase-related protein 3

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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