ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hydroxymethylglutaryl-CoA synthase, mitochondrial

Intermolecular
Cysteine 454 and cysteine 454
Intramolecular
Cysteine 305 and cysteine 389
Cysteine 106 and cysteine 194
Cysteine 166 and cysteine 194
A redox-regulated disulphide may form between two units of Hydroxymethylglutaryl-CoA synthase, mitochondrial at cysteines 454 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2wya
Structure name
crystal structure of human mitochondrial 3-hydroxy-3- methylglutaryl-coenzyme a synthase 2 (hmgcs2)
Structure deposition date
2009-11-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
68
Peptide A name
Hydroxymethylglutaryl-CoA synthase, mitochondrial
Peptide B name
Hydroxymethylglutaryl-CoA synthase, mitochondrial
Peptide A accession
P54868
Peptide B accession
P54868
Peptide A residue number
454
Peptide B residue number
454

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Hydroxymethylglutaryl-CoA synthase, mitochondrial between cysteines 305 and 389. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2wya
Structure name
crystal structure of human mitochondrial 3-hydroxy-3- methylglutaryl-coenzyme a synthase 2 (hmgcs2)
Structure deposition date
2009-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
100
Peptide accession
P54868
Residue number A
305
Residue number B
389
Peptide name
Hydroxymethylglutaryl-CoA synthase, mitochondrial

Ligandability

Cysteine 305 of Hydroxymethylglutaryl-CoA synthase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 389 of Hydroxymethylglutaryl-CoA synthase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Hydroxymethylglutaryl-CoA synthase, mitochondrial between cysteines 106 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2wya
Structure name
crystal structure of human mitochondrial 3-hydroxy-3- methylglutaryl-coenzyme a synthase 2 (hmgcs2)
Structure deposition date
2009-11-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
107
Minimum pKa ?
13
% buried
100
Peptide accession
P54868
Residue number A
106
Residue number B
194
Peptide name
Hydroxymethylglutaryl-CoA synthase, mitochondrial

Ligandability

Cysteine 106 of Hydroxymethylglutaryl-CoA synthase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 194 of Hydroxymethylglutaryl-CoA synthase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Hydroxymethylglutaryl-CoA synthase, mitochondrial between cysteines 166 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
18
PDB code
2wya
Structure name
crystal structure of human mitochondrial 3-hydroxy-3- methylglutaryl-coenzyme a synthase 2 (hmgcs2)
Structure deposition date
2009-11-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
104
Minimum pKa ?
13
% buried
100
Peptide accession
P54868
Residue number A
166
Residue number B
194
Peptide name
Hydroxymethylglutaryl-CoA synthase, mitochondrial

Ligandability

Cysteine 166 of Hydroxymethylglutaryl-CoA synthase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 194 of Hydroxymethylglutaryl-CoA synthase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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