ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Zinc finger and SCAN domain-containing protein 2

Intramolecular
Cysteine 588 and cysteine 255
Cysteine 336 and cysteine 255
A redox-regulated disulphide may form within Zinc finger and SCAN domain-containing protein 2 between cysteines 588 and 255 (136 and 139 respectively in this structure).

Details

Redox score ?
91
PDB code
2i13
Structure name
aart, a six finger zinc finger designed to recognize ann triplets
Structure deposition date
2006-08-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
5
% buried
0
Peptide accession
Q07230
Residue number A
588
Residue number B
255
Peptide name
Zinc finger and SCAN domain-containing protein 2

Ligandability

Cysteine 588 of Zinc finger and SCAN domain-containing protein 2

Cysteine 255 of Zinc finger and SCAN domain-containing protein 2

A redox-regulated disulphide may form within Zinc finger and SCAN domain-containing protein 2 between cysteines 336 and 255 (108 and 111 respectively in this structure).

Details

Redox score ?
87
PDB code
2i13
Structure name
aart, a six finger zinc finger designed to recognize ann triplets
Structure deposition date
2006-08-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
16
Peptide accession
Q07230
Residue number A
336
Residue number B
255
Peptide name
Zinc finger and SCAN domain-containing protein 2

Ligandability

Cysteine 336 of Zinc finger and SCAN domain-containing protein 2

Cysteine 255 of Zinc finger and SCAN domain-containing protein 2

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