ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolactin regulatory element-binding protein

Intramolecular
Cysteine 280 and cysteine 298
Cysteine 298 and cysteine 334
Cysteine 161 and cysteine 250
A redox-regulated disulphide may form within Prolactin regulatory element-binding protein between cysteines 280 and 298.

Details

Redox score ?
66
PDB code
5tf2
Structure name
crystal structure of the wd40 domain of the human prolactin regulatory element-binding protein
Structure deposition date
2016-09-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HCU5
Residue number A
280
Residue number B
298
Peptide name
Prolactin regulatory element-binding protein

Ligandability

Cysteine 280 of Prolactin regulatory element-binding protein

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 298 of Prolactin regulatory element-binding protein

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 regulatory element-binding protein between cysteines 298 and 334. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5tf2
Structure name
crystal structure of the wd40 domain of the human prolactin regulatory element-binding protein
Structure deposition date
2016-09-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HCU5
Residue number A
298
Residue number B
334
Peptide name
Prolactin regulatory element-binding protein

Ligandability

Cysteine 298 of Prolactin regulatory element-binding protein

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 334 of Prolactin regulatory element-binding protein

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 regulatory element-binding protein between cysteines 161 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5tf2
Structure name
crystal structure of the wd40 domain of the human prolactin regulatory element-binding protein
Structure deposition date
2016-09-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HCU5
Residue number A
161
Residue number B
250
Peptide name
Prolactin regulatory element-binding protein

Ligandability

Cysteine 161 of Prolactin regulatory element-binding protein

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 250 of Prolactin regulatory element-binding protein

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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