ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Choline O-acetyltransferase

Intramolecular
Cysteine 308 and cysteine 309
Cysteine 529 and cysteine 722
Cysteine 668 and cysteine 681
Cysteine 681 and cysteine 692
Cysteine 384 and cysteine 386
Cysteine 669 and cysteine 692
Cysteine 440 and cysteine 668
Cysteine 668 and cysteine 669
Cysteine 386 and cysteine 389
Cysteine 386 and cysteine 453
More...
Cysteine 440 and cysteine 453
Cysteine 384 and cysteine 389
Cysteine 668 and cysteine 692
Cysteine 308 and cysteine 389
Cysteine 669 and cysteine 681
Cysteine 440 and cysteine 669
A redox-regulated disulphide may form within Choline O-acetyltransferase between cysteines 308 and 309 (190 and 191 respectively in this structure).

Details

Redox score ?
71
PDB code
2fy3
Structure name
structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
6
% buried
78
Peptide accession
P28329
Residue number A
308
Residue number B
309
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 308 of Choline O-acetyltransferase

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 309 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 529 and 722 (411 and 604 respectively in this structure).

Details

Redox score ?
62
PDB code
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
62
Peptide accession
P28329
Residue number A
529
Residue number B
722
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 529 of Choline O-acetyltransferase

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 722 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 668 and 681 (550 and 563 respectively in this structure).

Details

Redox score ?
61
PDB code
2fy2
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
P28329
Residue number A
668
Residue number B
681
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 668 of Choline O-acetyltransferase

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 681 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 681 and 692 (563 and 574 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
10
% buried
100
Peptide accession
P28329
Residue number A
681
Residue number B
692
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 681 of Choline O-acetyltransferase

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 692 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 384 and 386 (266 and 268 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2fy4
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide accession
P28329
Residue number A
384
Residue number B
386
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 384 of Choline O-acetyltransferase

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 386 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 669 and 692 (551 and 574 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2fy2
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
98
Minimum pKa ?
13
% buried
100
Peptide accession
P28329
Residue number A
669
Residue number B
692
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 669 of Choline O-acetyltransferase

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 692 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 440 and 668 (322 and 550 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
97
Minimum pKa ?
8
% buried
100
Peptide accession
P28329
Residue number A
440
Residue number B
668
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 440 of Choline O-acetyltransferase

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 668 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 668 and 669 (550 and 551 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2fy2
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
101
Minimum pKa ?
13
% buried
100
Peptide accession
P28329
Residue number A
668
Residue number B
669
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 668 of Choline O-acetyltransferase

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 669 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 386 and 389 (268 and 271 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
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
P28329
Residue number A
386
Residue number B
389
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 386 of Choline O-acetyltransferase

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 389 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 386 and 453 (268 and 335 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2fy2
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
P28329
Residue number A
386
Residue number B
453
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 386 of Choline O-acetyltransferase

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 453 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 440 and 453 (322 and 335 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
P28329
Residue number A
440
Residue number B
453
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 440 of Choline O-acetyltransferase

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 453 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 384 and 389 (266 and 271 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
2fy2
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide accession
P28329
Residue number A
384
Residue number B
389
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 384 of Choline O-acetyltransferase

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 389 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 668 and 692 (550 and 574 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
2fy3
Structure name
structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
15
% buried
100
Peptide accession
P28329
Residue number A
668
Residue number B
692
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 668 of Choline O-acetyltransferase

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 692 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 308 and 389 (190 and 271 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
2fy4
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
96
Peptide accession
P28329
Residue number A
308
Residue number B
389
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 308 of Choline O-acetyltransferase

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 389 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 669 and 681 (551 and 563 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
97
Minimum pKa ?
18
% buried
100
Peptide accession
P28329
Residue number A
669
Residue number B
681
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 669 of Choline O-acetyltransferase

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 681 of Choline O-acetyltransferase

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 Choline O-acetyltransferase between cysteines 440 and 669 (322 and 551 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
18
PDB code
2fy5
Structure name
structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Structure deposition date
2006-02-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
102
Minimum pKa ?
14
% buried
100
Peptide accession
P28329
Residue number A
440
Residue number B
669
Peptide name
Choline O-acetyltransferase

Ligandability

Cysteine 440 of Choline O-acetyltransferase

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 669 of Choline O-acetyltransferase

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: