GTP-binding protein RAD

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of GTP-binding protein RAD at cysteines 221 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2gjs

Structure name

the crystal structure of human rrad in complex with gdp

Structure deposition date

2006-03-31

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

GTP-binding protein RAD

Peptide B name

GTP-binding protein RAD

Peptide A accession

P55042

Peptide B accession

P55042

Peptide A residue number

221

Peptide B residue number

221

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 GTP-binding protein RAD between cysteines 221 and 227. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?