a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein 292

Intramolecular

Cysteine 2116 and cysteine 2121

A redox-regulated disulphide may form within Zinc finger protein 292 between cysteines 2116 and 2121 (30 and 35 respectively in this structure).

Details

Redox score ?

89

PDB code

Structure name

solution structure of the c2h2 type zinc-binding domain of human zinc finger protein 292

Structure deposition date

2005-05-02

Thiol separation (Å)

4

Half-sphere exposure sum ?

39

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

2116

Residue number B

2121

Peptide name

Zinc finger protein 292

Ligandability

Cysteine 2116 of Zinc finger protein 292

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 2121 of Zinc finger protein 292

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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