ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Glutaryl-CoA dehydrogenase, mitochondrial

Intramolecular
Cysteine 228 and cysteine 232
Cysteine 350 and cysteine 375
A redox-regulated disulphide may form within Glutaryl-CoA dehydrogenase, mitochondrial between cysteines 228 and 232 (184 and 188 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
1siq
Structure name
the crystal structure and mechanism of human glutaryl-coa dehydrogenase
Structure deposition date
2004-03-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
25
Peptide accession
Q92947
Residue number A
228
Residue number B
232
Peptide name
Glutaryl-CoA dehydrogenase, mitochondrial

Ligandability

Cysteine 228 of Glutaryl-CoA dehydrogenase, mitochondrial

Cysteine 232 of Glutaryl-CoA dehydrogenase, mitochondrial

A redox-regulated disulphide may form within Glutaryl-CoA dehydrogenase, mitochondrial between cysteines 350 and 375 (306 and 331 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2r0m
Structure name
the effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate
Structure deposition date
2007-08-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
100
Peptide accession
Q92947
Residue number A
350
Residue number B
375
Peptide name
Glutaryl-CoA dehydrogenase, mitochondrial

Ligandability

Cysteine 350 of Glutaryl-CoA dehydrogenase, mitochondrial

Cysteine 375 of Glutaryl-CoA dehydrogenase, mitochondrial

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