ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Thymidine phosphorylase

Intramolecular
Cysteine 136 and cysteine 138
Cysteine 182 and cysteine 183
A redox-regulated disulphide may form within Thymidine phosphorylase between cysteines 136 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1uou
Structure name
crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor
Structure deposition date
2003-09-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
76
Peptide accession
P19971
Residue number A
136
Residue number B
138
Peptide name
Thymidine phosphorylase

Ligandability

Cysteine 136 of Thymidine phosphorylase

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 138 of Thymidine phosphorylase

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 Thymidine phosphorylase between cysteines 182 and 183. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2j0f
Structure name
structural basis for non-competitive product inhibition in human thymidine phosphorylase: implication for drug design
Structure deposition date
2006-08-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
12
% buried
100
Peptide accession
P19971
Residue number A
182
Residue number B
183
Peptide name
Thymidine phosphorylase

Ligandability

Cysteine 182 of Thymidine phosphorylase

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 183 of Thymidine phosphorylase

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.

If this tool was useful for finding a disulphide, please cite: