Protein Aster-C

Intramolecular

A redox-regulated disulphide may form within Protein Aster-C between cysteines 439 and 448. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6gn5

Structure name

crystal structure of human gramd1c start domain

Structure deposition date

2018-05-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q8IYS0

Residue number A

439

Residue number B

448

Peptide name

Protein Aster-C

Ligandability

Cysteine 439 of Protein Aster-C

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.