a tool for identifying drug-targetable redox-active disulphides

Interferon alpha-1/13

Intramolecular

Cysteine 52 and cysteine 162

A redox-regulated disulphide may form within Interferon alpha-1/13 between cysteines 52 and 162 (29 and 139 respectively in this structure).

Details

Redox score ?

80

PDB code

Structure name

structural insights into a human anti-ifn antibody exerting therapeutic potential for systemic lupus erythematosus

Structure deposition date

2011-12-04

Thiol separation (Å)

2

Half-sphere exposure sum ?

66

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

52

Residue number B

162

Peptide name

Interferon alpha-1/13

Ligandability

Cysteine 52 of Interferon alpha-1/13

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 alpha-1/13

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.

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