ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase epsilon

Intramolecular
Cysteine 253 and cysteine 262
Cysteine 262 and cysteine 278
Cysteine 253 and cysteine 278
Cysteine 536 and cysteine 630
Cysteine 244 and cysteine 335
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase epsilon between cysteines 253 and 262.

Details

Redox score ?
84
PDB code
2jjd
Structure name
protein tyrosine phosphatase, receptor type, e isoform
Structure deposition date
2008-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23469
Residue number A
253
Residue number B
262
Peptide name
Receptor-type tyrosine-protein phosphatase epsilon

Ligandability

Cysteine 253 of Receptor-type tyrosine-protein phosphatase epsilon

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 262 of Receptor-type tyrosine-protein phosphatase epsilon

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 Receptor-type tyrosine-protein phosphatase epsilon between cysteines 262 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2jjd
Structure name
protein tyrosine phosphatase, receptor type, e isoform
Structure deposition date
2008-03-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
nan
Peptide accession
P23469
Residue number A
262
Residue number B
278
Peptide name
Receptor-type tyrosine-protein phosphatase epsilon

Ligandability

Cysteine 262 of Receptor-type tyrosine-protein phosphatase epsilon

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 278 of Receptor-type tyrosine-protein phosphatase epsilon

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 Receptor-type tyrosine-protein phosphatase epsilon between cysteines 253 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2jjd
Structure name
protein tyrosine phosphatase, receptor type, e isoform
Structure deposition date
2008-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
nan
Peptide accession
P23469
Residue number A
253
Residue number B
278
Peptide name
Receptor-type tyrosine-protein phosphatase epsilon

Ligandability

Cysteine 253 of Receptor-type tyrosine-protein phosphatase epsilon

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 278 of Receptor-type tyrosine-protein phosphatase epsilon

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 Receptor-type tyrosine-protein phosphatase epsilon between cysteines 536 and 630. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2jjd
Structure name
protein tyrosine phosphatase, receptor type, e isoform
Structure deposition date
2008-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
95
Peptide accession
P23469
Residue number A
536
Residue number B
630
Peptide name
Receptor-type tyrosine-protein phosphatase epsilon

Ligandability

Cysteine 536 of Receptor-type tyrosine-protein phosphatase epsilon

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 630 of Receptor-type tyrosine-protein phosphatase epsilon

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 Receptor-type tyrosine-protein phosphatase epsilon between cysteines 244 and 335. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2jjd
Structure name
protein tyrosine phosphatase, receptor type, e isoform
Structure deposition date
2008-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
92
Peptide accession
P23469
Residue number A
244
Residue number B
335
Peptide name
Receptor-type tyrosine-protein phosphatase epsilon

Ligandability

Cysteine 244 of Receptor-type tyrosine-protein phosphatase epsilon

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 335 of Receptor-type tyrosine-protein phosphatase epsilon

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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