a tool for identifying drug-targetable redox-active disulphides

Interferon beta

Intramolecular

Cysteine 52 and cysteine 162

A redox-regulated disulphide may form within Interferon beta between cysteines 52 and 162 (31 and 141 respectively in this structure).

Details

Redox score ?

85

PDB code

Structure name

human interferon-beta crystal structure

Structure deposition date

1997-09-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

53

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

52

Residue number B

162

Peptide name

Interferon beta

Ligandability

Cysteine 52 of Interferon beta

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.

Cysteine 162 of Interferon beta

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.

If this tool was useful for finding a disulphide, please cite: