ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Follicle-stimulating hormone receptor

Intramolecular
Cysteine 18 and cysteine 25
Cysteine 292 and cysteine 338
Cysteine 276 and cysteine 356
Cysteine 23 and cysteine 32
Cysteine 275 and cysteine 346
Cysteine 275 and cysteine 276
Cysteine 23 and cysteine 25
Cysteine 275 and cysteine 356
Cysteine 346 and cysteine 356
Cysteine 276 and cysteine 346
Cysteine 25 and cysteine 32
A redox-regulated disulphide may form within Follicle-stimulating hormone receptor between cysteines 18 and 25.

Details

Redox score ?
92
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
18
Residue number B
25
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 18 of Follicle-stimulating hormone receptor

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 25 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 292 and 338.

Details

Redox score ?
88
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
32
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
292
Residue number B
338
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 292 of Follicle-stimulating hormone receptor

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 338 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 276 and 356.

Details

Redox score ?
86
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
276
Residue number B
356
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 276 of Follicle-stimulating hormone receptor

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 356 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 23 and 32.

Details

Redox score ?
84
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
23
Residue number B
32
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 23 of Follicle-stimulating hormone receptor

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 32 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 275 and 346.

Details

Redox score ?
81
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
38
Peptide accession
P23945
Residue number A
275
Residue number B
346
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 275 of Follicle-stimulating hormone receptor

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 346 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 275 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
nan
Peptide accession
P23945
Residue number A
275
Residue number B
276
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 275 of Follicle-stimulating hormone receptor

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 276 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 23 and 25. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
23
Residue number B
25
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 23 of Follicle-stimulating hormone receptor

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 25 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 275 and 356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
275
Residue number B
356
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 275 of Follicle-stimulating hormone receptor

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 356 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 346 and 356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
346
Residue number B
356
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 346 of Follicle-stimulating hormone receptor

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 356 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 276 and 346. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
276
Residue number B
346
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 276 of Follicle-stimulating hormone receptor

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 346 of Follicle-stimulating hormone receptor

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 Follicle-stimulating hormone receptor between cysteines 25 and 32. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23945
Residue number A
25
Residue number B
32
Peptide name
Follicle-stimulating hormone receptor

Ligandability

Cysteine 25 of Follicle-stimulating hormone receptor

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 32 of Follicle-stimulating hormone receptor

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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