Sestrin-2

Intramolecular

A redox-regulated disulphide may form within Sestrin-2 between cysteines 125 and 204. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5t0n

Structure name

pseudo-apo structure of sestrin2 at 3

Structure deposition date

2016-08-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P58004

Residue number A

125

Residue number B

204

Peptide name

Sestrin-2

Ligandability

Cysteine 125 of Sestrin-2

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.