ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Muellerian-inhibiting factor

Intramolecular
Cysteine 462 and cysteine 526
Cysteine 488 and cysteine 557
Cysteine 492 and cysteine 559
Cysteine 462 and cysteine 559
Cysteine 462 and cysteine 492
Cysteine 488 and cysteine 526
Cysteine 526 and cysteine 557
Cysteine 462 and cysteine 557
Cysteine 492 and cysteine 526
Cysteine 526 and cysteine 559
More...
Cysteine 462 and cysteine 488
Cysteine 492 and cysteine 525
Cysteine 525 and cysteine 526
Cysteine 462 and cysteine 525
Cysteine 525 and cysteine 559
Cysteine 488 and cysteine 559
Cysteine 557 and cysteine 559
Cysteine 488 and cysteine 492
Cysteine 488 and cysteine 525
Cysteine 492 and cysteine 557
A redox-regulated disulphide may form within Muellerian-inhibiting factor between cysteines 462 and 526.

Details

Redox score ?
86
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
462
Residue number B
526
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 462 of Muellerian-inhibiting factor

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 526 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 488 and 557.

Details

Redox score ?
86
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
488
Residue number B
557
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 488 of Muellerian-inhibiting factor

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 557 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 492 and 559.

Details

Redox score ?
84
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
492
Residue number B
559
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 492 of Muellerian-inhibiting factor

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 559 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 462 and 559.

Details

Redox score ?
74
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
462
Residue number B
559
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 462 of Muellerian-inhibiting factor

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 559 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 462 and 492.

Details

Redox score ?
71
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
462
Residue number B
492
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 462 of Muellerian-inhibiting factor

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 492 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 488 and 526.

Details

Redox score ?
70
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
488
Residue number B
526
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 488 of Muellerian-inhibiting factor

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 526 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 526 and 557.

Details

Redox score ?
69
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
526
Residue number B
557
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 526 of Muellerian-inhibiting factor

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 557 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 462 and 557.

Details

Redox score ?
67
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
462
Residue number B
557
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 462 of Muellerian-inhibiting factor

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 557 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 492 and 526.

Details

Redox score ?
67
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
492
Residue number B
526
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 492 of Muellerian-inhibiting factor

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 526 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 526 and 559.

Details

Redox score ?
67
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
526
Residue number B
559
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 526 of Muellerian-inhibiting factor

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 559 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 462 and 488.

Details

Redox score ?
66
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
462
Residue number B
488
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 462 of Muellerian-inhibiting factor

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 488 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 492 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
nan
Peptide accession
P03971
Residue number A
492
Residue number B
525
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 492 of Muellerian-inhibiting factor

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 525 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 525 and 526. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
nan
Peptide accession
P03971
Residue number A
525
Residue number B
526
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 525 of Muellerian-inhibiting factor

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 526 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 462 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
nan
Peptide accession
P03971
Residue number A
462
Residue number B
525
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 462 of Muellerian-inhibiting factor

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 525 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 525 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
nan
Peptide accession
P03971
Residue number A
525
Residue number B
559
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 525 of Muellerian-inhibiting factor

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 559 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 488 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
488
Residue number B
559
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 488 of Muellerian-inhibiting factor

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 559 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 557 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
557
Residue number B
559
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 557 of Muellerian-inhibiting factor

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 559 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 488 and 492. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
488
Residue number B
492
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 488 of Muellerian-inhibiting factor

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 492 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 488 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
nan
Peptide accession
P03971
Residue number A
488
Residue number B
525
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 488 of Muellerian-inhibiting factor

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 525 of Muellerian-inhibiting factor

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 Muellerian-inhibiting factor between cysteines 492 and 557. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03971
Residue number A
492
Residue number B
557
Peptide name
Muellerian-inhibiting factor

Ligandability

Cysteine 492 of Muellerian-inhibiting factor

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 557 of Muellerian-inhibiting factor

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: