Septin-2

Intramolecular

A redox-regulated disulphide may form within Septin-2 between cysteines 111 and 114. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3ftq

Structure name

crystal structure of septin 2 in complex with gppnhp and mg2+

Structure deposition date

2009-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P42208

Residue number A

111

Residue number B

114

Peptide name

Septin-2

Ligandability

Cysteine 111 of Septin-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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 114 of Septin-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.

A redox-regulated disulphide may form within Septin-2 between cysteines 148 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?