a tool for identifying drug-targetable redox-active disulphides

Glutathione S-transferase P

Intermolecular

Cysteine 102 and cysteine 102

A redox-regulated disulphide may form between two units of Glutathione S-transferase P at cysteines 102 and 102 (99 and 99 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

58

PDB code

Structure name

three-dimensional structure of class pi glutathione s-transferase from human placenta in complex with s-hexylglutathione at 2

Structure deposition date

1992-05-28

Thiol separation (Å)

5

Half-sphere exposure sum ?

45

Minimum pK_a ?

11

% buried

76

Peptide A name

Glutathione S-transferase P

Peptide B name

Glutathione S-transferase P

Peptide A accession

Peptide B accession

Peptide A residue number

102

Peptide B residue number

102

Ligandability

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: