ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Glucose-6-phosphate 1-dehydrogenase

Intramolecular
Cysteine 13 and cysteine 446 L
Cysteine 269 and cysteine 294
A redox-regulated disulphide may form within Glucose-6-phosphate 1-dehydrogenase between cysteines 13 and 446.

Details

Redox score ?
85
PDB code
1qki
Structure name
x-ray structure of human glucose 6-phosphate dehydrogenase (variant canton r459l) complexed with structural nadp+
Structure deposition date
1999-07-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P11413
Residue number A
13
Residue number B
446
Peptide name
Glucose-6-phosphate 1-dehydrogenase

Ligandability

Cysteine 13 of Glucose-6-phosphate 1-dehydrogenase

Cysteine 446 of Glucose-6-phosphate 1-dehydrogenase

A redox-regulated disulphide may form within Glucose-6-phosphate 1-dehydrogenase between cysteines 269 and 294. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2bhl
Structure name
x-ray structure of human glucose-6-phosphate dehydrogenase (deletion variant) complexed with glucose-6-phosphate
Structure deposition date
2005-01-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
73
Peptide accession
P11413
Residue number A
269
Residue number B
294
Peptide name
Glucose-6-phosphate 1-dehydrogenase

Ligandability

Cysteine 269 of Glucose-6-phosphate 1-dehydrogenase

Cysteine 294 of Glucose-6-phosphate 1-dehydrogenase

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