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 P62136
[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 (2)
| O35867 |
NEB1_RAT
Rattus norvegicus
Neurabin-1
|
| P62136 |
PP1A_HUMAN
Homo sapiens
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
|
PDB Structure
| PDB | 3HVQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites.
Nat.Struct.Mol.Biol.
|
