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 phosphatase 10 |
Enzyme Information
3.1.3.48 |
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q9Y6W6
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 Q9Y6W6
[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)
Q9Y6W6 |
DUS10_HUMAN
Homo sapiens
Dual specificity protein phosphatase 10
|
PDB Structure
PDB | 1ZZW |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase.
J.Mol.Biol.
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