Endophilin-A1

Intramolecular

A redox-regulated disulphide may form within Endophilin-A1 between cysteines 294 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3iql

Structure name

crystal structure of the rat endophilin-a1 sh3 domain

Structure deposition date

2009-08-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O35179

Residue number A

294

Residue number B

295

Peptide name

Endophilin-A1

Ligandability

Cysteine 294 of Endophilin-A1

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.