Septin-9

Intramolecular

A redox-regulated disulphide may form within Septin-9 between cysteines 410 and 411 (135 and 136 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5cyo

Structure name

high resolution septin 9 gtpase domain in complex with gdp

Structure deposition date

2015-07-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Q9UHD8

Residue number A

410

Residue number B

411

Peptide name

Septin-9

Ligandability

Cysteine 410 of Septin-9

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.