ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Acyl-protein thioesterase 1

Intermolecular
Cysteine 173 and cysteine 173
Cysteine 173 and cysteine 211
Cysteine 211 and cysteine 211
Intramolecular
Cysteine 169 and cysteine 211
Cysteine 144 and cysteine 169
A redox-regulated disulphide may form between two units of Acyl-protein thioesterase 1 at cysteines 173 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6qgn
Structure name
crystal structure of apt1 bound to 2-bromopalmitate
Structure deposition date
2019-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
11
% buried
30
Peptide A name
Acyl-protein thioesterase 1
Peptide B name
Acyl-protein thioesterase 1
Peptide A accession
O75608
Peptide B accession
O75608
Peptide A residue number
173
Peptide B residue number
173

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 between two units of Acyl-protein thioesterase 1 at cysteines 173 and 211 (168 and 206 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1fj2
Structure name
crystal structure of the human acyl protein thioesterase 1 at 1
Structure deposition date
2000-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
52
Peptide A name
Acyl-protein thioesterase 1
Peptide B name
Acyl-protein thioesterase 1
Peptide A accession
O75608
Peptide B accession
O75608
Peptide A residue number
173
Peptide B residue number
211

Ligandability

Cysteine 173 of Acyl-protein thioesterase 1

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 211 of Acyl-protein thioesterase 1

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 Acyl-protein thioesterase 1 at cysteines 211 and 211 (206 and 206 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1fj2
Structure name
crystal structure of the human acyl protein thioesterase 1 at 1
Structure deposition date
2000-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
70
Peptide A name
Acyl-protein thioesterase 1
Peptide B name
Acyl-protein thioesterase 1
Peptide A accession
O75608
Peptide B accession
O75608
Peptide A residue number
211
Peptide B residue number
211

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 Acyl-protein thioesterase 1 between cysteines 169 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6qgn
Structure name
crystal structure of apt1 bound to 2-bromopalmitate
Structure deposition date
2019-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
62
Peptide accession
O75608
Residue number A
169
Residue number B
211
Peptide name
Acyl-protein thioesterase 1

Ligandability

Cysteine 169 of Acyl-protein thioesterase 1

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 211 of Acyl-protein thioesterase 1

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 Acyl-protein thioesterase 1 between cysteines 144 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6qgo
Structure name
crystal structure of apt1 s119a mutant bound to palmitic acid
Structure deposition date
2019-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
99
Peptide accession
O75608
Residue number A
144
Residue number B
169
Peptide name
Acyl-protein thioesterase 1

Ligandability

Cysteine 144 of Acyl-protein thioesterase 1

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 169 of Acyl-protein thioesterase 1

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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