ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein 217

Intramolecular
Cysteine 501 and cysteine 504
Cysteine 473 and cysteine 476
A redox-regulated disulphide may form within Zinc finger protein 217 between cysteines 501 and 504.

Details

Redox score ?
88
PDB code
4is1
Structure name
crystal structure of znf217 bound to dna
Structure deposition date
2013-01-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
O75362
Residue number A
501
Residue number B
504
Peptide name
Zinc finger protein 217

Ligandability

Cysteine 501 of Zinc finger protein 217

Cysteine 504 of Zinc finger protein 217

A redox-regulated disulphide may form within Zinc finger protein 217 between cysteines 473 and 476.

Details

Redox score ?
88
PDB code
3uk3
Structure name
crystal structure of znf217 bound to dna
Structure deposition date
2011-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
2
Peptide accession
O75362
Residue number A
473
Residue number B
476
Peptide name
Zinc finger protein 217

Ligandability

Cysteine 473 of Zinc finger protein 217

Cysteine 476 of Zinc finger protein 217

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