14-3-3 protein epsilon

Intramolecular

A redox-regulated disulphide may form within 14-3-3 protein epsilon between cysteines 97 and 98. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3ual

Structure name

crystal structure of 14-3-3 epsilon with mlf1 peptide

Structure deposition date

2011-10-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P62258

Residue number A

Residue number B

Peptide name

14-3-3 protein epsilon

Ligandability

Cysteine 97 of 14-3-3 protein epsilon

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.