ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-citrate synthase

Intermolecular
Cysteine 913 and cysteine 913
Intramolecular
Cysteine 293 and cysteine 748
Cysteine 742 and cysteine 744
Cysteine 728 and cysteine 742
Cysteine 519 and cysteine 633 L
Cysteine 887 and cysteine 1040
Cysteine 744 and cysteine 748
Cysteine 728 and cysteine 744
A redox-regulated disulphide may form between two units of ATP-citrate synthase at cysteines 913 and 913. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6hxl
Structure name
structure of the citryl-coa lyase core module of human atp citrate lyase in complex with citrate and coash (space group p21)
Structure deposition date
2018-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
103
Minimum pKa ?
11
% buried
100
Peptide A name
ATP-citrate synthase
Peptide B name
ATP-citrate synthase
Peptide A accession
P53396
Peptide B accession
P53396
Peptide A residue number
913
Peptide B residue number
913

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 ATP-citrate synthase between cysteines 293 and 748.

Details

Redox score ?
80
PDB code
6qfb
Structure name
structure of the human atp citrate lyase holoenzyme in complex with citrate, coenzyme a and mg
Structure deposition date
2019-01-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
54
Peptide accession
P53396
Residue number A
293
Residue number B
748
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 293 of ATP-citrate 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 748 of ATP-citrate 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 ATP-citrate synthase between cysteines 742 and 744.

Details

Redox score ?
65
PDB code
6qfb
Structure name
structure of the human atp citrate lyase holoenzyme in complex with citrate, coenzyme a and mg
Structure deposition date
2019-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
93
Peptide accession
P53396
Residue number A
742
Residue number B
744
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 742 of ATP-citrate 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 744 of ATP-citrate 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 ATP-citrate synthase between cysteines 728 and 742. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6hxh
Structure name
structure of the human atp citrate lyase holoenzyme in complex with citrate, coenzyme a and mg
Structure deposition date
2018-10-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
74
Peptide accession
P53396
Residue number A
728
Residue number B
742
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 728 of ATP-citrate 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 742 of ATP-citrate 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 ATP-citrate synthase between cysteines 519 and 633. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6hxh
Structure name
structure of the human atp citrate lyase holoenzyme in complex with citrate, coenzyme a and mg
Structure deposition date
2018-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
78
Peptide accession
P53396
Residue number A
519
Residue number B
633
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 519 of ATP-citrate 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 633 of ATP-citrate 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 ATP-citrate synthase between cysteines 887 and 1040. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6hxl
Structure name
structure of the citryl-coa lyase core module of human atp citrate lyase in complex with citrate and coash (space group p21)
Structure deposition date
2018-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
65
Peptide accession
P53396
Residue number A
887
Residue number B
1040
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 887 of ATP-citrate 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 1040 of ATP-citrate 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 ATP-citrate synthase between cysteines 744 and 748. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6uv5
Structure name
structure of human atp citrate lyase in complex with acetyl-coa and oxaloacetate
Structure deposition date
2019-11-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
51
Peptide accession
P53396
Residue number A
744
Residue number B
748
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 744 of ATP-citrate 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 748 of ATP-citrate 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 ATP-citrate synthase between cysteines 728 and 744. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6hxh
Structure name
structure of the human atp citrate lyase holoenzyme in complex with citrate, coenzyme a and mg
Structure deposition date
2018-10-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
73
Peptide accession
P53396
Residue number A
728
Residue number B
744
Peptide name
ATP-citrate synthase

Ligandability

Cysteine 728 of ATP-citrate 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 744 of ATP-citrate 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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