CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.90 | Alpha-Beta Complex | 
|   | 3.90.190 | Protein-Tyrosine Phosphatase; Chain A | 
|   | 3.90.190.10 | Protein tyrosine phosphatase superfamily | 
Domain Context
CATH Clusters
| Superfamily | Protein tyrosine phosphatase superfamily | 
| Functional Family | Dual specificity protein phosphatase 3 | 
Enzyme Information
| 3.1.3.48 | Protein-tyrosine-phosphatase. based on mapping to UniProt P51452 Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. -!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2. | 
| 3.1.3.16 | Protein-serine/threonine phosphatase. based on mapping to UniProt P51452 [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. -!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1). | 
UniProtKB Entries (1)
| P51452 | DUS3_HUMAN Homo sapiens Dual specificity protein phosphatase 3 | 
PDB Structure
| PDB | 1J4X | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase. Biochemistry | 
