ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein 423

Intramolecular
Cysteine 961 and cysteine 964
Cysteine 932 and cysteine 935
A redox-regulated disulphide may form within Zinc finger protein 423 between cysteines 961 and 964 (35 and 38 respectively in this structure).

Details

Redox score ?
89
PDB code
2mdg
Structure name
solution nmr structure of zinc finger protein 423 from homo sapiens, northeast structural genomics consortium (nesg) target hr7298f
Structure deposition date
2013-09-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
6
% buried
0
Peptide accession
Q2M1K9
Residue number A
961
Residue number B
964
Peptide name
Zinc finger protein 423

Ligandability

Cysteine 961 of Zinc finger protein 423

Cysteine 964 of Zinc finger protein 423

A redox-regulated disulphide may form within Zinc finger protein 423 between cysteines 932 and 935 (6 and 9 respectively in this structure).

Details

Redox score ?
86
PDB code
2mdg
Structure name
solution nmr structure of zinc finger protein 423 from homo sapiens, northeast structural genomics consortium (nesg) target hr7298f
Structure deposition date
2013-09-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
0
Peptide accession
Q2M1K9
Residue number A
932
Residue number B
935
Peptide name
Zinc finger protein 423

Ligandability

Cysteine 932 of Zinc finger protein 423

Cysteine 935 of Zinc finger protein 423

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