a tool for identifying drug-targetable redox-active disulphides

Arfaptin-2

Intramolecular

Cysteine 10 and cysteine 28

A redox-regulated disulphide may form within Arfaptin-2 between cysteines 10 and 28.

Details

Redox score ?

nan

PDB code

Structure name

s1p4 first extracellular loop peptidomimetic

Structure deposition date

2006-01-11

Thiol separation (Å)

2

Half-sphere exposure sum ?

52

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

10

Residue number B

28

Peptide name

Arfaptin-2

Ligandability

Cysteine 10 of Arfaptin-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.

Cysteine 28 of Arfaptin-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.

Cysteine 10 in protein A could not be asigned to a Uniprot residue.

Cysteine 28 in protein B could not be asigned to a Uniprot residue.

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