ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Tyrosine-protein phosphatase non-receptor type 3

Intramolecular
Cysteine 725 and cysteine 754
Cysteine 774 and cysteine 779
Cysteine 754 and cysteine 842
A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type 3 between cysteines 725 and 754. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4rh5
Structure name
crystal structure of ptpn3 (ptph1) in complex with eps15 ptyr849 peptide
Structure deposition date
2014-10-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
86
Peptide accession
P26045
Residue number A
725
Residue number B
754
Peptide name
Tyrosine-protein phosphatase non-receptor type 3

Ligandability

Cysteine 725 of Tyrosine-protein phosphatase non-receptor type 3

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 754 of Tyrosine-protein phosphatase non-receptor type 3

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 3 between cysteines 774 and 779. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4ri4
Structure name
crystal structure of ptpn3 (ptph1) y676i mutant in complex with vanadate
Structure deposition date
2014-10-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P26045
Residue number A
774
Residue number B
779
Peptide name
Tyrosine-protein phosphatase non-receptor type 3

Ligandability

Cysteine 774 of Tyrosine-protein phosphatase non-receptor type 3

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 779 of Tyrosine-protein phosphatase non-receptor type 3

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 3 between cysteines 754 and 842. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2b49
Structure name
crystal structure of the catalytic domain of protein tyrosine phosphatase, non-receptor type 3
Structure deposition date
2005-09-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
98
Peptide accession
P26045
Residue number A
754
Residue number B
842
Peptide name
Tyrosine-protein phosphatase non-receptor type 3

Ligandability

Cysteine 754 of Tyrosine-protein phosphatase non-receptor type 3

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 842 of Tyrosine-protein phosphatase non-receptor type 3

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.

If this tool was useful for finding a disulphide, please cite: