ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

protein-serine/threonine phosphatase

Intramolecular
Cysteine 272 and cysteine 294
Cysteine 71 and cysteine 149
A redox-regulated disulphide may form within protein-serine/threonine phosphatase between cysteines 272 and 294. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2p8e
Structure name
crystal structure of the serine/threonine phosphatase domain of human ppm1b
Structure deposition date
2007-03-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
92
Peptide accession
Q4J6C0
Residue number A
272
Residue number B
294
Peptide name
protein-serine/threonine phosphatase

Ligandability

Cysteine 272 of protein-serine/threonine phosphatase

Cysteine 294 of protein-serine/threonine phosphatase

A redox-regulated disulphide may form within protein-serine/threonine phosphatase between cysteines 71 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2p8e
Structure name
crystal structure of the serine/threonine phosphatase domain of human ppm1b
Structure deposition date
2007-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q4J6C0
Residue number A
71
Residue number B
149
Peptide name
protein-serine/threonine phosphatase

Ligandability

Cysteine 71 of protein-serine/threonine phosphatase

Cysteine 149 of protein-serine/threonine phosphatase

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