a tool for identifying drug-targetable redox-active disulphides

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Intramolecular

Cysteine 71 and cysteine 124

A redox-regulated disulphide may form within Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN between cysteines 71 and 124. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

57

PDB code

Structure name

crystal structure of pten (aa 7-353 followed by spacer tgggsggtgggsggtgggcy ligated to peptide psdptptdpsdpenepfded)

Structure deposition date

2020-08-24

Thiol separation (Å)

6

Half-sphere exposure sum ?

77

Minimum pK_a ?

9

% buried

87

Peptide accession

Residue number A

71

Residue number B

124

Peptide name

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Ligandability

Cysteine 71 of Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

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 124 of Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

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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