CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.40 | Phosphatase 2c; domain 1 |
|
3.60.40.10 | PPM-type phosphatase domain |
Domain Context
CATH Clusters
| Superfamily | PPM-type phosphatase domain |
| Functional Family | Protein phosphatase 1A |
Enzyme Information
| 3.1.3.16 |
Protein-serine/threonine phosphatase.
based on mapping to UniProt P35813
[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)
| P35813 |
PPM1A_HUMAN
Homo sapiens
Protein phosphatase 1A
|
PDB Structure
| PDB | 6B67 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.
J. Biol. Chem.
|