ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Fatty acid synthase

Intermolecular
Cysteine 2292 and cysteine 2292 L
Intramolecular
Cysteine 630 and cysteine 634
Cysteine 496 and cysteine 587
Cysteine 1315 and cysteine 1317
Cysteine 212 and cysteine 223 L
Cysteine 1459 and cysteine 2024
Cysteine 1127 and cysteine 1227
Cysteine 587 and cysteine 593
Cysteine 1227 and cysteine 1403
Cysteine 161 and cysteine 212
A redox-regulated disulphide may form between two units of Fatty acid synthase at cysteines 2292 and 2292. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4z49
Structure name
homo sapiens fatty acid synthetase, thioesterase domain at 1
Structure deposition date
2015-04-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
100
Peptide A name
Fatty acid synthase
Peptide B name
Fatty acid synthase
Peptide A accession
P49327
Peptide B accession
P49327
Peptide A residue number
2292
Peptide B residue number
2292

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Fatty acid synthase between cysteines 630 and 634.

Details

Redox score ?
82
PDB code
3hhd
Structure name
structure of the human fatty acid synthase ks-mat didomain as a framework for inhibitor design
Structure deposition date
2009-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
56
Peptide accession
P49327
Residue number A
630
Residue number B
634
Peptide name
Fatty acid synthase

Ligandability

Cysteine 630 of Fatty acid synthase

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 634 of Fatty acid synthase

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 Fatty acid synthase between cysteines 496 and 587.

Details

Redox score ?
66
PDB code
6rop
Structure name
ks-mat di-domain of mouse fas with octanoyl coa
Structure deposition date
2019-05-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
P19096
Residue number A
496
Residue number B
587
Peptide name
Fatty acid synthase

Ligandability

Cysteine 496 of Fatty acid synthase

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 587 of Fatty acid synthase

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 Fatty acid synthase between cysteines 1315 and 1317.

Details

Redox score ?
61
PDB code
6nna
Structure name
human fatty acid synthase psi/kr tri-domain with nadph and compound 22
Structure deposition date
2019-01-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
100
Peptide accession
P49327
Residue number A
1315
Residue number B
1317
Peptide name
Fatty acid synthase

Ligandability

Cysteine 1315 of Fatty acid synthase

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 1317 of Fatty acid synthase

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 Fatty acid synthase between cysteines 212 and 223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3hhd
Structure name
structure of the human fatty acid synthase ks-mat didomain as a framework for inhibitor design
Structure deposition date
2009-05-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P49327
Residue number A
212
Residue number B
223
Peptide name
Fatty acid synthase

Ligandability

Cysteine 212 of Fatty acid synthase

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 223 of Fatty acid synthase

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Fatty acid synthase between cysteines 1459 and 2024. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4piv
Structure name
human fatty acid synthase psi/kr tri-domain with nadph and gsk2194069
Structure deposition date
2014-05-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
P49327
Residue number A
1459
Residue number B
2024
Peptide name
Fatty acid synthase

Ligandability

Cysteine 1459 of Fatty acid synthase

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 2024 of Fatty acid synthase

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 Fatty acid synthase between cysteines 1127 and 1227. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5c37
Structure name
structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor
Structure deposition date
2015-06-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
74
Peptide accession
P49327
Residue number A
1127
Residue number B
1227
Peptide name
Fatty acid synthase

Ligandability

Cysteine 1127 of Fatty acid synthase

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 1227 of Fatty acid synthase

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 Fatty acid synthase between cysteines 587 and 593. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2jfd
Structure name
structure of the mat domain of human fas
Structure deposition date
2007-01-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
76
Peptide accession
P49327
Residue number A
587
Residue number B
593
Peptide name
Fatty acid synthase

Ligandability

Cysteine 587 of Fatty acid synthase

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 593 of Fatty acid synthase

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 Fatty acid synthase between cysteines 1227 and 1403. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
4piv
Structure name
human fatty acid synthase psi/kr tri-domain with nadph and gsk2194069
Structure deposition date
2014-05-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
100
Peptide accession
P49327
Residue number A
1227
Residue number B
1403
Peptide name
Fatty acid synthase

Ligandability

Cysteine 1227 of Fatty acid synthase

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 1403 of Fatty acid synthase

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 Fatty acid synthase between cysteines 161 and 212. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
6rop
Structure name
ks-mat di-domain of mouse fas with octanoyl coa
Structure deposition date
2019-05-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
P19096
Residue number A
161
Residue number B
212
Peptide name
Fatty acid synthase

Ligandability

Cysteine 161 of Fatty acid synthase

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 212 of Fatty acid synthase

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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