a tool for identifying drug-targetable redox-active disulphides

Peptidyl-prolyl cis-trans isomerase

Intramolecular

Cysteine 107 and cysteine 160

A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase between cysteines 107 and 160 (62 and 115 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

30

PDB code

Structure name

structure of the n-terminal capsid domain of hiv-2

Structure deposition date

2009-06-26

Thiol separation (Å)

10

Half-sphere exposure sum ?

84

Minimum pK_a ?

11

% buried

82

Peptide accession

Residue number A

107

Residue number B

160

Peptide name

Peptidyl-prolyl cis-trans isomerase

Ligandability

Cysteine 107 of Peptidyl-prolyl cis-trans isomerase

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 160 of Peptidyl-prolyl cis-trans isomerase

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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