Peptidyl-prolyl cis-trans isomerase

Intramolecular

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

Details

Redox score ?

PDB code

5lud

Structure name

structure of cyclophilin a in complex with 2,3-diaminopyridine

Structure deposition date

2016-09-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

V9HWF5

Residue number A

Residue number B

115

Peptide name

Peptidyl-prolyl cis-trans isomerase

Ligandability

Cysteine 62 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.