ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolactin

Intramolecular
Cysteine 23 and cysteine 39
Cysteine 32 and cysteine 39
Cysteine 4 and cysteine 39
Cysteine 219 and cysteine 227
Cysteine 86 and cysteine 202
A redox-regulated disulphide may form within Prolactin between cysteines 23 and 39 (4 and 11 respectively in this structure).

Details

Redox score ?
94
PDB code
3npz
Structure name
prolactin receptor (prlr) complexed with the natural hormone (prl)
Structure deposition date
2010-06-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01236
Residue number A
23
Residue number B
39
Peptide name
Prolactin

Ligandability

Cysteine 23 of Prolactin

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 39 of Prolactin

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 between cysteines 32 and 39 (4 and 11 respectively in this structure).

Details

Redox score ?
91
PDB code
1rw5
Structure name
solution structure of human prolactin
Structure deposition date
2003-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
25
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01236
Residue number A
32
Residue number B
39
Peptide name
Prolactin

Ligandability

Cysteine 32 of Prolactin

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 39 of Prolactin

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 between cysteines 4 and 39 (4 and 11 respectively in this structure).

Details

Redox score ?
89
PDB code
3ew3
Structure name
the 1:2 complex between a nterminal elongated prolactin and the extra cellular domain of the rat prolactin receptor
Structure deposition date
2008-10-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01236
Residue number A
4
Residue number B
39
Peptide name
Prolactin

Ligandability

Cysteine 4 of Prolactin

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 39 of Prolactin

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 4 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Prolactin between cysteines 219 and 227 (191 and 199 respectively in this structure).

Details

Redox score ?
88
PDB code
3npz
Structure name
prolactin receptor (prlr) complexed with the natural hormone (prl)
Structure deposition date
2010-06-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01236
Residue number A
219
Residue number B
227
Peptide name
Prolactin

Ligandability

Cysteine 219 of Prolactin

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 227 of Prolactin

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 between cysteines 86 and 202 (58 and 174 respectively in this structure).

Details

Redox score ?
83
PDB code
3ew3
Structure name
the 1:2 complex between a nterminal elongated prolactin and the extra cellular domain of the rat prolactin receptor
Structure deposition date
2008-10-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01236
Residue number A
86
Residue number B
202
Peptide name
Prolactin

Ligandability

Cysteine 86 of Prolactin

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 202 of Prolactin

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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