Gephyrin

Intramolecular

A redox-regulated disulphide may form within Gephyrin between cysteines 133 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1jlj

Structure name

Structure deposition date

2001-07-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q9NQX3

Residue number A

133

Residue number B

154

Peptide name

Gephyrin

Ligandability

Cysteine 133 of Gephyrin

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.