Excision repair cross-complementing rodent repair deficiency, complementation group 6 variant

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Excision repair cross-complementing rodent repair deficiency, complementation group 6 variant at cysteines 841 and 841 (1464 and 1464 respectively in this structure).

Details

Redox score ?

PDB code

6a6i

Structure name

crystal structure of the winged-helix domain of cockayne syndrome group b protein in complex with ubiquitin

Structure deposition date

2018-06-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Excision repair cross-complementing rodent repair deficiency, complementation group 6 variant

Peptide B name

Excision repair cross-complementing rodent repair deficiency, complementation group 6 variant

Peptide A accession

Q59FF6

Peptide B accession

Q59FF6

Peptide A residue number

841

Peptide B residue number

841

Ligandability

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.

A redox-regulated disulphide may form within Excision repair cross-complementing rodent repair deficiency, complementation group 6 variant between cysteines 851 and 870 (1474 and 1493 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?