a tool for identifying drug-targetable redox-active disulphides

Zinc fingers and homeoboxes protein 3

Intramolecular

Cysteine 514 and cysteine 549

A redox-regulated disulphide may form within Zinc fingers and homeoboxes protein 3 between cysteines 514 and 549 (28 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

49

PDB code

Structure name

solution structure of the second homeobox domain of human zinc fingers and homeoboxes protein 3

Structure deposition date

2006-04-24

Thiol separation (Å)

9

Half-sphere exposure sum ?

26

Minimum pK_a ?

9

% buried

0

Peptide accession

Residue number A

514

Residue number B

549

Peptide name

Zinc fingers and homeoboxes protein 3

Ligandability

Cysteine 514 of Zinc fingers and homeoboxes protein 3

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 549 of Zinc fingers and homeoboxes protein 3

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: