ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase S

Intramolecular
Cysteine 266 and cysteine 311
Cysteine 156 and cysteine 216
Cysteine 54 and cysteine 107
Cysteine 1548 and cysteine 1557
Cysteine 1501 and cysteine 1589
Cysteine 1790 and cysteine 1880
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase S between cysteines 266 and 311 (253 and 298 respectively in this structure).

Details

Redox score ?
83
PDB code
4pbx
Structure name
crystal structure of the six n-terminal domains of human receptor protein tyrosine phosphatase sigma
Structure deposition date
2014-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13332
Residue number A
266
Residue number B
311
Peptide name
Receptor-type tyrosine-protein phosphatase S

Ligandability

Cysteine 266 of Receptor-type tyrosine-protein phosphatase S

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 311 of Receptor-type tyrosine-protein phosphatase S

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 S between cysteines 156 and 216 (156 and 207 respectively in this structure).

Details

Redox score ?
80
PDB code
4pbx
Structure name
crystal structure of the six n-terminal domains of human receptor protein tyrosine phosphatase sigma
Structure deposition date
2014-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13332
Residue number A
156
Residue number B
216
Peptide name
Receptor-type tyrosine-protein phosphatase S

Ligandability

Cysteine 156 of Receptor-type tyrosine-protein phosphatase S

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 216 of Receptor-type tyrosine-protein phosphatase S

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 S between cysteines 54 and 107.

Details

Redox score ?
80
PDB code
4pbx
Structure name
crystal structure of the six n-terminal domains of human receptor protein tyrosine phosphatase sigma
Structure deposition date
2014-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13332
Residue number A
54
Residue number B
107
Peptide name
Receptor-type tyrosine-protein phosphatase S

Ligandability

Cysteine 54 of Receptor-type tyrosine-protein phosphatase S

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 107 of Receptor-type tyrosine-protein phosphatase S

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 S between cysteines 1548 and 1557. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3sr9
Structure name
crystal structure of mouse ptpsigma
Structure deposition date
2011-07-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
7
% buried
100
Peptide accession
B0V2N1
Residue number A
1548
Residue number B
1557
Peptide name
Receptor-type tyrosine-protein phosphatase S

Ligandability

Cysteine 1548 of Receptor-type tyrosine-protein phosphatase S

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 1557 of Receptor-type tyrosine-protein phosphatase S

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 S between cysteines 1501 and 1589. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2fh7
Structure name
crystal structure of the phosphatase domains of human ptp sigma
Structure deposition date
2005-12-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
100
Peptide accession
Q13332
Residue number A
1501
Residue number B
1589
Peptide name
Receptor-type tyrosine-protein phosphatase S

Ligandability

Cysteine 1501 of Receptor-type tyrosine-protein phosphatase S

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 1589 of Receptor-type tyrosine-protein phosphatase S

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 S between cysteines 1790 and 1880. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4bpc
Structure name
structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form
Structure deposition date
2013-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
98
Peptide accession
Q13332
Residue number A
1790
Residue number B
1880
Peptide name
Receptor-type tyrosine-protein phosphatase S

Ligandability

Cysteine 1790 of Receptor-type tyrosine-protein phosphatase S

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 1880 of Receptor-type tyrosine-protein phosphatase S

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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