a tool for identifying drug-targetable redox-active disulphides

Histidine-rich glycoprotein

Intramolecular

Cysteine 207 and cysteine 230

A redox-regulated disulphide may form within Histidine-rich glycoprotein between cysteines 207 and 230 (199 and 222 respectively in this structure).

Details

Redox score ?

88

PDB code

Structure name

crystal structure of histidine-rich glycoprotein n2 domain reveals redox activity at an interdomain disulfide bridge: implications for the regulation of angiogenesis

Structure deposition date

2013-10-29

Thiol separation (Å)

2

Half-sphere exposure sum ?

69

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

207

Residue number B

230

Peptide name

Histidine-rich glycoprotein

Ligandability

Cysteine 207 of Histidine-rich glycoprotein

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 230 of Histidine-rich glycoprotein

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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