ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein 24

Intramolecular
Cysteine 309 and cysteine 312
Cysteine 281 and cysteine 284
A redox-regulated disulphide may form within Zinc finger protein 24 between cysteines 309 and 312 (45 and 48 respectively in this structure).

Details

Redox score ?
88
PDB code
1x6e
Structure name
solution structures of the c2h2 type zinc finger domain of human zinc finger protein 24
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
P17028
Residue number A
309
Residue number B
312
Peptide name
Zinc finger protein 24

Ligandability

Cysteine 309 of Zinc finger protein 24

Cysteine 312 of Zinc finger protein 24

A redox-regulated disulphide may form within Zinc finger protein 24 between cysteines 281 and 284 (17 and 20 respectively in this structure).

Details

Redox score ?
86
PDB code
1x6e
Structure name
solution structures of the c2h2 type zinc finger domain of human zinc finger protein 24
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
P17028
Residue number A
281
Residue number B
284
Peptide name
Zinc finger protein 24

Ligandability

Cysteine 281 of Zinc finger protein 24

Cysteine 284 of Zinc finger protein 24

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