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 6 |
Enzyme Information
| 3.1.3.48 |
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q16828
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 Q16828
[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)
| Q16828 |
DUS6_HUMAN
Homo sapiens
Dual specificity protein phosphatase 6
|
PDB Structure
| PDB | 1MKP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation.
Nat.Struct.Biol.
|
