ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolactin receptor

Intramolecular
Cysteine 36 and cysteine 46
Cysteine 75 and cysteine 86
Cysteine 46 and cysteine 86
Cysteine 46 and cysteine 75
Cysteine 36 and cysteine 86
A redox-regulated disulphide may form within Prolactin receptor between cysteines 36 and 46 (12 and 22 respectively in this structure).

Details

Redox score ?
83
PDB code
3n06
Structure name
a mutant human prolactin receptor antagonist h27a in complex with the extracellular domain of the human prolactin receptor
Structure deposition date
2010-05-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16471
Residue number A
36
Residue number B
46
Peptide name
Prolactin receptor

Ligandability

Cysteine 36 of Prolactin 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 46 of Prolactin 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 Prolactin receptor between cysteines 75 and 86 (51 and 62 respectively in this structure).

Details

Redox score ?
83
PDB code
4i18
Structure name
crystal structure of human prolactin receptor complexed with fab fragment
Structure deposition date
2012-11-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16471
Residue number A
75
Residue number B
86
Peptide name
Prolactin receptor

Ligandability

Cysteine 75 of Prolactin 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 86 of Prolactin 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 Prolactin receptor between cysteines 46 and 86 (22 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3n0p
Structure name
a mutant human prolactin receptor antagonist h30a in complex with the extracellular domain of the human prolactin receptor
Structure deposition date
2010-05-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16471
Residue number A
46
Residue number B
86
Peptide name
Prolactin receptor

Ligandability

Cysteine 46 of Prolactin 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 86 of Prolactin 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 Prolactin receptor between cysteines 46 and 75 (22 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3d48
Structure name
crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor
Structure deposition date
2008-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16471
Residue number A
46
Residue number B
75
Peptide name
Prolactin receptor

Ligandability

Cysteine 46 of Prolactin 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 75 of Prolactin 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 Prolactin receptor between cysteines 36 and 86 (12 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3nce
Structure name
a mutant human prolactin receptor antagonist h27a in complex with the mutant extracellular domain h188a of the human prolactin receptor
Structure deposition date
2010-06-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16471
Residue number A
36
Residue number B
86
Peptide name
Prolactin receptor

Ligandability

Cysteine 36 of Prolactin 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 86 of Prolactin 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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