a tool for identifying drug-targetable redox-active disulphides

Amphiphysin

Intramolecular

Cysteine 102 and cysteine 224

A redox-regulated disulphide may form within Amphiphysin between cysteines 102 and 224.

Details

Redox score ?

61

PDB code

Structure name

crystal structure of the bar domain of human amphiphysin, isoform 1 at 1

Structure deposition date

2012-05-08

Thiol separation (Å)

6

Half-sphere exposure sum ?

59

Minimum pK_a ?

10

% buried

31

Peptide accession

Residue number A

102

Residue number B

224

Peptide name

Amphiphysin

Ligandability

Cysteine 102 of Amphiphysin

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 224 of Amphiphysin

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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