ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Peroxisomal carnitine O-octanoyltransferase

Intramolecular
Cysteine 196 and cysteine 228
Cysteine 107 and cysteine 323
Cysteine 323 and cysteine 325
Cysteine 437 and cysteine 458
Cysteine 324 and cysteine 325
Cysteine 458 and cysteine 466
Cysteine 437 and cysteine 438
Cysteine 323 and cysteine 324
Cysteine 438 and cysteine 458
Cysteine 107 and cysteine 325
A redox-regulated disulphide may form within Peroxisomal carnitine O-octanoyltransferase between cysteines 196 and 228.

Details

Redox score ?
78
PDB code
1xl8
Structure name
crystal structure of mouse carnitine octanoyltransferase in complex with octanoylcarnitine
Structure deposition date
2004-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
66
Peptide accession
Q9DC50
Residue number A
196
Residue number B
228
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 196 of Peroxisomal carnitine O-octanoyltransferase

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 228 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 107 and 323.

Details

Redox score ?
67
PDB code
1xl7
Structure name
crystal structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
100
Peptide accession
Q9DC50
Residue number A
107
Residue number B
323
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 107 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 323 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1xl8
Structure name
crystal structure of mouse carnitine octanoyltransferase in complex with octanoylcarnitine
Structure deposition date
2004-09-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
100
Peptide accession
Q9DC50
Residue number A
323
Residue number B
325
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 323 of Peroxisomal carnitine O-octanoyltransferase

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 325 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 437 and 458. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1xl7
Structure name
crystal structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-09-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
95
Peptide accession
Q9DC50
Residue number A
437
Residue number B
458
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 437 of Peroxisomal carnitine O-octanoyltransferase

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 458 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 324 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1xmc
Structure name
c323m mutant structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-10-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
11
% buried
100
Peptide accession
Q9DC50
Residue number A
324
Residue number B
325
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 324 of Peroxisomal carnitine O-octanoyltransferase

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 325 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 458 and 466. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1xl8
Structure name
crystal structure of mouse carnitine octanoyltransferase in complex with octanoylcarnitine
Structure deposition date
2004-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q9DC50
Residue number A
458
Residue number B
466
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 458 of Peroxisomal carnitine O-octanoyltransferase

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 466 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 437 and 438. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1xmd
Structure name
m335v mutant structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-10-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
92
Peptide accession
Q9DC50
Residue number A
437
Residue number B
438
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 437 of Peroxisomal carnitine O-octanoyltransferase

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 438 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 323 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1xl7
Structure name
crystal structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-09-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
Q9DC50
Residue number A
323
Residue number B
324
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 323 of Peroxisomal carnitine O-octanoyltransferase

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 324 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 438 and 458. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1xl7
Structure name
crystal structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
Q9DC50
Residue number A
438
Residue number B
458
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 438 of Peroxisomal carnitine O-octanoyltransferase

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 458 of Peroxisomal carnitine O-octanoyltransferase

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 Peroxisomal carnitine O-octanoyltransferase between cysteines 107 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
20
PDB code
1xl7
Structure name
crystal structure of mouse carnitine octanoyltransferase
Structure deposition date
2004-09-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
14
% buried
100
Peptide accession
Q9DC50
Residue number A
107
Residue number B
325
Peptide name
Peroxisomal carnitine O-octanoyltransferase

Ligandability

Cysteine 107 of Peroxisomal carnitine O-octanoyltransferase

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 325 of Peroxisomal carnitine O-octanoyltransferase

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.

If this tool was useful for finding a disulphide, please cite: