ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Acyloxyacyl hydrolase

Intermolecular
Cysteine 123 and cysteine 453
Cysteine 41 and cysteine 453
Cysteine 114 and cysteine 453
Intramolecular
Cysteine 160 and cysteine 169 L
Cysteine 41 and cysteine 114
Cysteine 70 and cysteine 83
Cysteine 122 and cysteine 452
Cysteine 249 and cysteine 329 L
Cysteine 376 and cysteine 459
Cysteine 44 and cysteine 108
More...
Cysteine 206 and cysteine 230
Cysteine 108 and cysteine 114
Cysteine 44 and cysteine 114
Cysteine 41 and cysteine 123
Cysteine 41 and cysteine 108
Cysteine 41 and cysteine 44
Cysteine 114 and cysteine 123
Cysteine 40 and cysteine 452
Cysteine 113 and cysteine 452
A redox-regulated disulphide may form between two units of Acyloxyacyl hydrolase at cysteines 123 and 453.

Details

Redox score ?
81
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Acyloxyacyl hydrolase
Peptide B name
Acyloxyacyl hydrolase
Peptide A accession
P28039
Peptide B accession
P28039
Peptide A residue number
123
Peptide B residue number
453

Ligandability

Cysteine 123 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase at cysteines 41 and 453. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide A name
Acyloxyacyl hydrolase
Peptide B name
Acyloxyacyl hydrolase
Peptide A accession
P28039
Peptide B accession
P28039
Peptide A residue number
41
Peptide B residue number
453

Ligandability

Cysteine 41 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase at cysteines 114 and 453. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5w78
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed
Structure deposition date
2017-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
Acyloxyacyl hydrolase
Peptide B name
Acyloxyacyl hydrolase
Peptide A accession
P28039
Peptide B accession
P28039
Peptide A residue number
114
Peptide B residue number
453

Ligandability

Cysteine 114 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 160 and 169.

Details

Redox score ?
85
PDB code
5w78
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
160
Residue number B
169
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 160 of Acyloxyacyl hydrolase

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.

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 Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 41 and 114.

Details

Redox score ?
85
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
41
Residue number B
114
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 41 of Acyloxyacyl hydrolase

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 114 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 70 and 83.

Details

Redox score ?
83
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
70
Residue number B
83
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 70 of Acyloxyacyl hydrolase

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 83 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 122 and 452.

Details

Redox score ?
81
PDB code
5w7f
Structure name
murine acyloxyacyl hydrolase (aoah), s262a mutant, with lipid a
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35298
Residue number A
122
Residue number B
452
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 122 of Acyloxyacyl hydrolase

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 452 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 249 and 329.

Details

Redox score ?
81
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
249
Residue number B
329
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 249 of Acyloxyacyl hydrolase

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.

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 329 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 376 and 459.

Details

Redox score ?
80
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
376
Residue number B
459
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 376 of Acyloxyacyl hydrolase

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 459 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 44 and 108.

Details

Redox score ?
80
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
44
Residue number B
108
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 44 of Acyloxyacyl hydrolase

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 108 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 206 and 230.

Details

Redox score ?
79
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
206
Residue number B
230
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 206 of Acyloxyacyl hydrolase

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 230 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 108 and 114.

Details

Redox score ?
67
PDB code
5w78
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed
Structure deposition date
2017-06-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
108
Residue number B
114
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 108 of Acyloxyacyl hydrolase

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 114 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 44 and 114.

Details

Redox score ?
62
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
44
Residue number B
114
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 44 of Acyloxyacyl hydrolase

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 114 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 41 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
41
Residue number B
123
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 41 of Acyloxyacyl hydrolase

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 123 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 41 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5w78
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed
Structure deposition date
2017-06-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
41
Residue number B
108
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 41 of Acyloxyacyl hydrolase

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 108 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 41 and 44. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5w7c
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed, s263a mutant, with lps
Structure deposition date
2017-06-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
41
Residue number B
44
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 41 of Acyloxyacyl hydrolase

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 44 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 114 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5w78
Structure name
human acyloxyacyl hydrolase (aoah), proteolytically processed
Structure deposition date
2017-06-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P28039
Residue number A
114
Residue number B
123
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 114 of Acyloxyacyl hydrolase

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 123 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 40 and 452. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5w7e
Structure name
murine acyloxyacyl hydrolase (aoah), s262a mutant, with dimyristoyl phosphatidylcholine
Structure deposition date
2017-06-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35298
Residue number A
40
Residue number B
452
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 40 of Acyloxyacyl hydrolase

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 452 of Acyloxyacyl hydrolase

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 Acyloxyacyl hydrolase between cysteines 113 and 452. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5w7f
Structure name
murine acyloxyacyl hydrolase (aoah), s262a mutant, with lipid a
Structure deposition date
2017-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35298
Residue number A
113
Residue number B
452
Peptide name
Acyloxyacyl hydrolase

Ligandability

Cysteine 113 of Acyloxyacyl hydrolase

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 452 of Acyloxyacyl hydrolase

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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