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 alpha-3 isoform |
Enzyme Information
| 2.7.11.19 |
Phosphorylase kinase.
based on mapping to UniProt P62161
2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
-!- Requires calmodulin for activity. -!- The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. -!- For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. -!- The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b. -!- The gamma subunit of the tetrameric alpha-beta-gamma-delta enzyme is the catalytic subunit. -!- Formerly EC 2.7.1.38.
|
| 3.1.3.16 |
Protein-serine/threonine phosphatase.
based on mapping to UniProt P63329
[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)
| P63100 |
CANB1_RAT
Rattus norvegicus
Calcineurin subunit B type 1
|
PDB Structure
| PDB | 4IL1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis of calcineurin activation by calmodulin.
Cell Signal
|