ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

3-alpha-hydroxysteroid dehydrogenase

Intramolecular
Cysteine 188 and cysteine 206
A redox-regulated disulphide may form within 3-alpha-hydroxysteroid dehydrogenase between cysteines 188 and 206. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
1lwi
Structure name
3-alpha-hydroxysteroid/dihydrodiol dehydrogenase from rattus norvegicus
Structure deposition date
1996-02-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
86
Peptide accession
P23457
Residue number A
188
Residue number B
206
Peptide name
3-alpha-hydroxysteroid dehydrogenase

Ligandability

Cysteine 188 of 3-alpha-hydroxysteroid dehydrogenase

Cysteine 206 of 3-alpha-hydroxysteroid dehydrogenase

If this tool was useful for finding a disulphide, please cite: