Peptidyl-prolyl cis-trans isomerase FKBP8

Intramolecular

A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase FKBP8 between cysteines 178 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2awg

Structure name

structure of the ppiase domain of the human fk506-binding protein 8

Structure deposition date

2005-09-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q14318

Residue number A

178

Residue number B

195

Peptide name

Peptidyl-prolyl cis-trans isomerase FKBP8

Ligandability

Cysteine 178 of Peptidyl-prolyl cis-trans isomerase FKBP8

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.