Elongation factor 1-gamma

Intramolecular

A redox-regulated disulphide may form within Elongation factor 1-gamma between cysteines 166 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5jpo

Structure name

complex structure of human elongation factor 1b gamma gst-liked domain and delta n-terminal domain

Structure deposition date

2016-05-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P26641

Residue number A

166

Residue number B

194

Peptide name

Elongation factor 1-gamma

Ligandability

Cysteine 166 of Elongation factor 1-gamma

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 194 of Elongation factor 1-gamma

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.

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