a tool for identifying drug-targetable redox-active disulphides

Acetyl-coenzyme A thioesterase

Intermolecular

Cysteine 270 and cysteine 51

Cysteine 40 and cysteine 270

Intramolecular

Cysteine 40 and cysteine 51

Cysteine 221 and cysteine 258

A redox-regulated disulphide may form between two units of Acetyl-coenzyme A thioesterase at cysteines 270 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

49

PDB code

Structure name

human acyl-coenzyme a thioesterase 12

Structure deposition date

2007-10-31

Thiol separation (Å)

7

Half-sphere exposure sum ?

75

Minimum pK_a ?

11

% buried

85

Peptide A name

Acetyl-coenzyme A thioesterase

Peptide B name

Acetyl-coenzyme A thioesterase

Peptide A accession

Peptide B accession

Peptide A residue number

270

Peptide B residue number

51

Ligandability

Cysteine 270 of Acetyl-coenzyme A thioesterase

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 51 of Acetyl-coenzyme A thioesterase

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 between two units of Acetyl-coenzyme A thioesterase at cysteines 40 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

human acyl-coenzyme a thioesterase 12

Structure deposition date

2007-10-31

Thiol separation (Å)

8

Half-sphere exposure sum ?

88

Minimum pK_a ?

11

% buried

85

Peptide A name

Acetyl-coenzyme A thioesterase

Peptide B name

Acetyl-coenzyme A thioesterase

Peptide A accession

Peptide B accession

Peptide A residue number

40

Peptide B residue number

270

Ligandability

Cysteine 40 of Acetyl-coenzyme A thioesterase

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 270 of Acetyl-coenzyme A thioesterase

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 Acetyl-coenzyme A thioesterase between cysteines 40 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

human acyl-coenzyme a thioesterase 12

Structure deposition date

2007-10-31

Thiol separation (Å)

6

Half-sphere exposure sum ?

92

Minimum pK_a ?

14

% buried

100

Peptide accession

Residue number A

40

Residue number B

51

Peptide name

Acetyl-coenzyme A thioesterase

Ligandability

Cysteine 40 of Acetyl-coenzyme A thioesterase

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 51 of Acetyl-coenzyme A thioesterase

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 Acetyl-coenzyme A thioesterase between cysteines 221 and 258. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

human acyl-coenzyme a thioesterase 12

Structure deposition date

2007-10-31

Thiol separation (Å)

9

Half-sphere exposure sum ?

66

Minimum pK_a ?

10

% buried

48

Peptide accession

Residue number A

221

Residue number B

258

Peptide name

Acetyl-coenzyme A thioesterase

Ligandability

Cysteine 221 of Acetyl-coenzyme A thioesterase

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 258 of Acetyl-coenzyme A thioesterase

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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