CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.21 | Purple Acid Phosphatase; chain A, domain 2 |
|
3.60.21.10 | Metallo-dependent phosphatases |
Domain Context
CATH Clusters
| Superfamily | 3.60.21.10 |
| Functional Family | Serine/threonine-protein phosphatase |
Enzyme Information
| 3.1.3.16 |
Protein-serine/threonine phosphatase.
based on mapping to UniProt P62207
[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).
|
| 3.1.3.53 |
[Myosin-light-chain] phosphatase.
based on mapping to UniProt P62207
[Myosin light-chain] phosphate + H(2)O = [myosin light-chain] + phosphate.
-!- Composed of three subunits. -!- The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.31, but not myosin; the catalytic subunit acts on all three substrates.
|
UniProtKB Entries (1)
| Q90623 |
MYPT1_CHICK
Gallus gallus
Protein phosphatase 1 regulatory subunit 12A
|
PDB Structure
| PDB | 1S70 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis of protein phosphatase 1 regulation
Nature
|
