GTP-binding protein REM 1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of GTP-binding protein REM 1 at cysteines 213 and 213. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2nzj

Structure name

the crystal structure of rem1 in complex with gdp

Structure deposition date

2006-11-23

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

GTP-binding protein REM 1

Peptide B name

GTP-binding protein REM 1

Peptide A accession

O75628

Peptide B accession

O75628

Peptide A residue number

213

Peptide B residue number

213

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 REM 1 between cysteines 213 and 219. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?