ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Dual specificity protein phosphatase 6

Intramolecular
Cysteine 90 and cysteine 127
Cysteine 39 and cysteine 147
A redox-regulated disulphide may form within Dual specificity protein phosphatase 6 between cysteines 90 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
1hzm
Structure name
structure of erk2 binding domain of mapk phosphatase mkp-3: structural insights into mkp-3 activation by erk2
Structure deposition date
2001-01-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
25
Peptide accession
Q16828
Residue number A
90
Residue number B
127
Peptide name
Dual specificity protein phosphatase 6

Ligandability

Cysteine 90 of Dual specificity protein phosphatase 6

Cysteine 127 of Dual specificity protein phosphatase 6

A redox-regulated disulphide may form within Dual specificity protein phosphatase 6 between cysteines 39 and 147. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1hzm
Structure name
structure of erk2 binding domain of mapk phosphatase mkp-3: structural insights into mkp-3 activation by erk2
Structure deposition date
2001-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
76
Peptide accession
Q16828
Residue number A
39
Residue number B
147
Peptide name
Dual specificity protein phosphatase 6

Ligandability

Cysteine 39 of Dual specificity protein phosphatase 6

Cysteine 147 of Dual specificity protein phosphatase 6

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