ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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3-hydroxy-3-methylglutaryl-coenzyme A reductase

Intermolecular
Cysteine 708 and cysteine 600
Cysteine 561 and cysteine 527
Cysteine 526 and cysteine 561
Intramolecular
Cysteine 176 and cysteine 198
Cysteine 708 and cysteine 843
Cysteine 777 and cysteine 795
Cysteine 195 and cysteine 198
Cysteine 795 and cysteine 843
Cysteine 777 and cysteine 843
Cysteine 708 and cysteine 795
More...
Cysteine 764 and cysteine 817
Cysteine 194 and cysteine 198
Cysteine 526 and cysteine 527
Cysteine 194 and cysteine 195
Cysteine 545 and cysteine 570
Cysteine 176 and cysteine 195
Cysteine 708 and cysteine 777
A redox-regulated disulphide may form between two units of 3-hydroxy-3-methylglutaryl-coenzyme A reductase at cysteines 708 and 600. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3cda
Structure name
thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
Structure deposition date
2008-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
76
Peptide A name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Peptide B name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Peptide A accession
P04035
Peptide B accession
P04035
Peptide A residue number
708
Peptide B residue number
600

Ligandability

Cysteine 708 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 600 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase at cysteines 561 and 527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3cda
Structure name
thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
Structure deposition date
2008-02-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
66
Peptide A name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Peptide B name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Peptide A accession
P04035
Peptide B accession
P04035
Peptide A residue number
561
Peptide B residue number
527

Ligandability

Cysteine 561 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 527 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase at cysteines 526 and 561. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3cda
Structure name
thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
Structure deposition date
2008-02-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
52
Peptide A name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Peptide B name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Peptide A accession
P04035
Peptide B accession
P04035
Peptide A residue number
526
Peptide B residue number
561

Ligandability

Cysteine 526 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 561 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 176 and 198.

Details

Redox score ?
65
PDB code
8djk
Structure name
hmgcr-ubiad1 complex state 2
Structure deposition date
2022-06-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
94
Peptide accession
P00347
Residue number A
176
Residue number B
198
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 176 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 198 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 708 and 843.

Details

Redox score ?
65
PDB code
1hwi
Structure name
complex of the catalytic portion of human hmg-coa reductase with fluvastatin
Structure deposition date
2001-01-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
96
Minimum pKa ?
11
% buried
100
Peptide accession
P04035
Residue number A
708
Residue number B
843
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 708 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 843 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 777 and 795. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
1dq9
Structure name
complex of catalytic portion of human hmg-coa reductase with hmg-coa
Structure deposition date
1999-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
104
Minimum pKa ?
11
% buried
100
Peptide accession
P04035
Residue number A
777
Residue number B
795
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 777 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 795 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 195 and 198. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
8djm
Structure name
hmgcr-ubiad1 complex state 1
Structure deposition date
2022-07-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
65
Peptide accession
P00347
Residue number A
195
Residue number B
198
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 195 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 198 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 795 and 843. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1dq9
Structure name
complex of catalytic portion of human hmg-coa reductase with hmg-coa
Structure deposition date
1999-12-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
102
Minimum pKa ?
10
% buried
100
Peptide accession
P04035
Residue number A
795
Residue number B
843
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 795 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 843 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 777 and 843. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1dqa
Structure name
complex of the catalytic portion of human hmg-coa reductase with hmg, coa, and nadp+
Structure deposition date
1999-12-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
103
Minimum pKa ?
10
% buried
100
Peptide accession
P04035
Residue number A
777
Residue number B
843
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 777 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 843 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 708 and 795. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
1dqa
Structure name
complex of the catalytic portion of human hmg-coa reductase with hmg, coa, and nadp+
Structure deposition date
1999-12-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
95
Minimum pKa ?
15
% buried
100
Peptide accession
P04035
Residue number A
708
Residue number B
795
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 708 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 795 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 764 and 817. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2q6b
Structure name
design and synthesis of novel, conformationally restricted hmg-coa reductase inhibitors
Structure deposition date
2007-06-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
102
Minimum pKa ?
13
% buried
100
Peptide accession
P04035
Residue number A
764
Residue number B
817
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 764 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 817 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 194 and 198. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
8djm
Structure name
hmgcr-ubiad1 complex state 1
Structure deposition date
2022-07-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
13
% buried
88
Peptide accession
P00347
Residue number A
194
Residue number B
198
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 194 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 198 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 526 and 527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1dq8
Structure name
complex of the catalytic portion of human hmg-coa reductase with hmg and coa
Structure deposition date
1999-12-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
88
Peptide accession
P04035
Residue number A
526
Residue number B
527
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 526 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 527 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 194 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
8djm
Structure name
hmgcr-ubiad1 complex state 1
Structure deposition date
2022-07-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
66
Peptide accession
P00347
Residue number A
194
Residue number B
195
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 194 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 195 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 545 and 570. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3cda
Structure name
thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
Structure deposition date
2008-02-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
62
Peptide accession
P04035
Residue number A
545
Residue number B
570
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 545 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 570 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 176 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
8djk
Structure name
hmgcr-ubiad1 complex state 2
Structure deposition date
2022-06-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
74
Peptide accession
P00347
Residue number A
176
Residue number B
195
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 176 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 195 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 3-hydroxy-3-methylglutaryl-coenzyme A reductase between cysteines 708 and 777. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1hwi
Structure name
complex of the catalytic portion of human hmg-coa reductase with fluvastatin
Structure deposition date
2001-01-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
10
% buried
100
Peptide accession
P04035
Residue number A
708
Residue number B
777
Peptide name
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Ligandability

Cysteine 708 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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 777 of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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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