ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase kappa

Intramolecular
Cysteine 1144 and cysteine 1152
Cysteine 1142 and cysteine 1144
Cysteine 995 and cysteine 1082
Cysteine 1082 and cysteine 1091
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase kappa between cysteines 1144 and 1152 (1145 and 1153 respectively in this structure).

Details

Redox score ?
88
PDB code
2c7s
Structure name
crystal structure of human protein tyrosine phosphatase kappa at 1
Structure deposition date
2005-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15262
Residue number A
1144
Residue number B
1152
Peptide name
Receptor-type tyrosine-protein phosphatase kappa

Ligandability

Cysteine 1144 of Receptor-type tyrosine-protein phosphatase kappa

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 1152 of Receptor-type tyrosine-protein phosphatase kappa

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 kappa between cysteines 1142 and 1144 (1143 and 1145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2c7s
Structure name
crystal structure of human protein tyrosine phosphatase kappa at 1
Structure deposition date
2005-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
nan
Peptide accession
Q15262
Residue number A
1142
Residue number B
1144
Peptide name
Receptor-type tyrosine-protein phosphatase kappa

Ligandability

Cysteine 1142 of Receptor-type tyrosine-protein phosphatase kappa

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 1144 of Receptor-type tyrosine-protein phosphatase kappa

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 kappa between cysteines 995 and 1082 (996 and 1083 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2c7s
Structure name
crystal structure of human protein tyrosine phosphatase kappa at 1
Structure deposition date
2005-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
100
Peptide accession
Q15262
Residue number A
995
Residue number B
1082
Peptide name
Receptor-type tyrosine-protein phosphatase kappa

Ligandability

Cysteine 995 of Receptor-type tyrosine-protein phosphatase kappa

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 1082 of Receptor-type tyrosine-protein phosphatase kappa

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 kappa between cysteines 1082 and 1091 (1083 and 1092 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2c7s
Structure name
crystal structure of human protein tyrosine phosphatase kappa at 1
Structure deposition date
2005-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
Q15262
Residue number A
1082
Residue number B
1091
Peptide name
Receptor-type tyrosine-protein phosphatase kappa

Ligandability

Cysteine 1082 of Receptor-type tyrosine-protein phosphatase kappa

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 1091 of Receptor-type tyrosine-protein phosphatase kappa

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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