a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein 462

Intramolecular

Cysteine 1894 and cysteine 1897

A redox-regulated disulphide may form within Zinc finger protein 462 between cysteines 1894 and 1897 (28 and 31 respectively in this structure).

Details

Redox score ?

86

PDB code

Structure name

solution structures of the c2h2 type zinc finger domain of human zinc finger protein 462

Structure deposition date

2005-05-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

35

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

1894

Residue number B

1897

Peptide name

Zinc finger protein 462

Ligandability

Cysteine 1894 of Zinc finger protein 462

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 1897 of Zinc finger protein 462

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: