ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Dual specificity phosphatase 28

Intramolecular
Cysteine 40 and cysteine 91
Cysteine 91 and cysteine 106
Cysteine 78 and cysteine 91
Cysteine 78 and cysteine 106
Cysteine 95 and cysteine 106
A redox-regulated disulphide may form within Dual specificity phosphatase 28 between cysteines 40 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2hcm
Structure name
crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, new york structural genomics consortium
Structure deposition date
2006-06-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BTR5
Residue number A
40
Residue number B
91
Peptide name
Dual specificity phosphatase 28

Ligandability

Cysteine 40 of Dual specificity phosphatase 28

Cysteine 91 of Dual specificity phosphatase 28

A redox-regulated disulphide may form within Dual specificity phosphatase 28 between cysteines 91 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2hcm
Structure name
crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, new york structural genomics consortium
Structure deposition date
2006-06-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BTR5
Residue number A
91
Residue number B
106
Peptide name
Dual specificity phosphatase 28

Ligandability

Cysteine 91 of Dual specificity phosphatase 28

Cysteine 106 of Dual specificity phosphatase 28

A redox-regulated disulphide may form within Dual specificity phosphatase 28 between cysteines 78 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2hcm
Structure name
crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, new york structural genomics consortium
Structure deposition date
2006-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BTR5
Residue number A
78
Residue number B
91
Peptide name
Dual specificity phosphatase 28

Ligandability

Cysteine 78 of Dual specificity phosphatase 28

Cysteine 91 of Dual specificity phosphatase 28

A redox-regulated disulphide may form within Dual specificity phosphatase 28 between cysteines 78 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2hcm
Structure name
crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, new york structural genomics consortium
Structure deposition date
2006-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BTR5
Residue number A
78
Residue number B
106
Peptide name
Dual specificity phosphatase 28

Ligandability

Cysteine 78 of Dual specificity phosphatase 28

Cysteine 106 of Dual specificity phosphatase 28

A redox-regulated disulphide may form within Dual specificity phosphatase 28 between cysteines 95 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2hcm
Structure name
crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, new york structural genomics consortium
Structure deposition date
2006-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BTR5
Residue number A
95
Residue number B
106
Peptide name
Dual specificity phosphatase 28

Ligandability

Cysteine 95 of Dual specificity phosphatase 28

Cysteine 106 of Dual specificity phosphatase 28

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