CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.238 | Recoverin; domain 1 |
|
1.10.238.10 | EF-hand |
Domain Context
CATH Clusters
| Superfamily | EF-hand |
| Functional Family |
Enzyme Information
| 2.7.11.19 |
Phosphorylase kinase.
based on mapping to UniProt P62149
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.
|
UniProtKB Entries (1)
| P11716 |
RYR1_RABIT
Oryctolagus cuniculus
Ryanodine receptor 1
|
PDB Structure
| PDB | 2BCX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode.
Structure
|