ADP-ribosylhydrolase ARH1

Intramolecular

A redox-regulated disulphide may form within ADP-ribosylhydrolase ARH1 between cysteines 137 and 312. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6g2a

Structure name

human [protein adp-ribosylargenine] hydrolase arh1 in complex with adp-hpm

Structure deposition date

2018-03-22

Thiol separation (Å)

Half-sphere exposure sum ?

116

Minimum pK_a ?

% buried

100

Peptide accession

P54922

Residue number A

137

Residue number B

312

Peptide name

ADP-ribosylhydrolase ARH1

Ligandability

Cysteine 137 of ADP-ribosylhydrolase ARH1

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.