ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase-like N

Intramolecular
Cysteine 803 and cysteine 903
Cysteine 803 and cysteine 897
Cysteine 820 and cysteine 909
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase-like N between cysteines 803 and 903. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2i1y
Structure name
crystal structure of the phosphatase domain of human ptp ia-2
Structure deposition date
2006-08-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
60
Peptide accession
Q16849
Residue number A
803
Residue number B
903
Peptide name
Receptor-type tyrosine-protein phosphatase-like N

Ligandability

Cysteine 803 of Receptor-type tyrosine-protein phosphatase-like N

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 903 of Receptor-type tyrosine-protein phosphatase-like N

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-like N between cysteines 803 and 897. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2i1y
Structure name
crystal structure of the phosphatase domain of human ptp ia-2
Structure deposition date
2006-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
75
Peptide accession
Q16849
Residue number A
803
Residue number B
897
Peptide name
Receptor-type tyrosine-protein phosphatase-like N

Ligandability

Cysteine 803 of Receptor-type tyrosine-protein phosphatase-like N

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 897 of Receptor-type tyrosine-protein phosphatase-like N

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-like N between cysteines 820 and 909. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2i1y
Structure name
crystal structure of the phosphatase domain of human ptp ia-2
Structure deposition date
2006-08-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
98
Peptide accession
Q16849
Residue number A
820
Residue number B
909
Peptide name
Receptor-type tyrosine-protein phosphatase-like N

Ligandability

Cysteine 820 of Receptor-type tyrosine-protein phosphatase-like N

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 909 of Receptor-type tyrosine-protein phosphatase-like N

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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