ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase T

Intramolecular
Cysteine 1144 and cysteine 1146
Cysteine 997 and cysteine 1084
Cysteine 1084 and cysteine 1093
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase T between cysteines 1144 and 1146 (1166 and 1168 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2ooq
Structure name
crystal structure of the human receptor phosphatase ptprt
Structure deposition date
2007-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
19
Peptide accession
O14522
Residue number A
1144
Residue number B
1146
Peptide name
Receptor-type tyrosine-protein phosphatase T

Ligandability

Cysteine 1144 of Receptor-type tyrosine-protein phosphatase T

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 1146 of Receptor-type tyrosine-protein phosphatase T

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 T between cysteines 997 and 1084 (1019 and 1106 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2ooq
Structure name
crystal structure of the human receptor phosphatase ptprt
Structure deposition date
2007-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
97
Peptide accession
O14522
Residue number A
997
Residue number B
1084
Peptide name
Receptor-type tyrosine-protein phosphatase T

Ligandability

Cysteine 997 of Receptor-type tyrosine-protein phosphatase T

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 1084 of Receptor-type tyrosine-protein phosphatase T

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 T between cysteines 1084 and 1093 (1106 and 1115 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2ooq
Structure name
crystal structure of the human receptor phosphatase ptprt
Structure deposition date
2007-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
8
% buried
100
Peptide accession
O14522
Residue number A
1084
Residue number B
1093
Peptide name
Receptor-type tyrosine-protein phosphatase T

Ligandability

Cysteine 1084 of Receptor-type tyrosine-protein phosphatase T

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 1093 of Receptor-type tyrosine-protein phosphatase T

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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