ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tyrosine-protein phosphatase non-receptor type 2

Intramolecular
Cysteine 94 and cysteine 123
Cysteine 94 and cysteine 95
Cysteine 123 and cysteine 216
A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type 2 between cysteines 94 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7f5n
Structure name
crystal structure of tcptp catalytic domain
Structure deposition date
2021-06-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
88
Peptide accession
P17706
Residue number A
94
Residue number B
123
Peptide name
Tyrosine-protein phosphatase non-receptor type 2

Ligandability

Cysteine 94 of Tyrosine-protein phosphatase non-receptor type 2

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 123 of Tyrosine-protein phosphatase non-receptor type 2

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 Tyrosine-protein phosphatase non-receptor type 2 between cysteines 94 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7f5o
Structure name
crystal structure of ptpn2 catalytic domain
Structure deposition date
2021-06-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
64
Peptide accession
P17706
Residue number A
94
Residue number B
95
Peptide name
Tyrosine-protein phosphatase non-receptor type 2

Ligandability

Cysteine 94 of Tyrosine-protein phosphatase non-receptor type 2

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 95 of Tyrosine-protein phosphatase non-receptor type 2

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 Tyrosine-protein phosphatase non-receptor type 2 between cysteines 123 and 216. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7f5n
Structure name
crystal structure of tcptp catalytic domain
Structure deposition date
2021-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
100
Peptide accession
P17706
Residue number A
123
Residue number B
216
Peptide name
Tyrosine-protein phosphatase non-receptor type 2

Ligandability

Cysteine 123 of Tyrosine-protein phosphatase non-receptor type 2

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 Tyrosine-protein phosphatase non-receptor type 2

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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