Geranylgeranyl pyrophosphate synthase

Intramolecular

A redox-regulated disulphide may form within Geranylgeranyl pyrophosphate synthase between cysteines 205 and 247. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6g32

Structure name

crystal structure of human geranylgeranyl diphosphate synthase mutant d188y

Structure deposition date

2018-03-24

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O95749

Residue number A

205

Residue number B

247

Peptide name

Geranylgeranyl pyrophosphate synthase

Ligandability

Cysteine 205 of Geranylgeranyl pyrophosphate synthase

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 247 of Geranylgeranyl pyrophosphate synthase

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 Geranylgeranyl pyrophosphate synthase between cysteines 138 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?