ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hydroxymethylglutaryl-CoA lyase, mitochondrial

Intramolecular
Cysteine 170 and cysteine 174
Cysteine 307 and cysteine 323
Cysteine 170 and cysteine 266
A redox-regulated disulphide may form within Hydroxymethylglutaryl-CoA lyase, mitochondrial between cysteines 170 and 174.

Details

Redox score ?
73
PDB code
2cw6
Structure name
crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria
Structure deposition date
2005-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
29
Peptide accession
P35914
Residue number A
170
Residue number B
174
Peptide name
Hydroxymethylglutaryl-CoA lyase, mitochondrial

Ligandability

Cysteine 170 of Hydroxymethylglutaryl-CoA lyase, 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 174 of Hydroxymethylglutaryl-CoA lyase, 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 lyase, mitochondrial between cysteines 307 and 323. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3mp3
Structure name
crystal structure of human lyase in complex with inhibitor hg-coa
Structure deposition date
2010-04-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
36
Peptide accession
P35914
Residue number A
307
Residue number B
323
Peptide name
Hydroxymethylglutaryl-CoA lyase, mitochondrial

Ligandability

Cysteine 307 of Hydroxymethylglutaryl-CoA lyase, 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 323 of Hydroxymethylglutaryl-CoA lyase, 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 lyase, mitochondrial between cysteines 170 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3mp3
Structure name
crystal structure of human lyase in complex with inhibitor hg-coa
Structure deposition date
2010-04-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
74
Peptide accession
P35914
Residue number A
170
Residue number B
266
Peptide name
Hydroxymethylglutaryl-CoA lyase, mitochondrial

Ligandability

Cysteine 170 of Hydroxymethylglutaryl-CoA lyase, 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 266 of Hydroxymethylglutaryl-CoA lyase, 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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