CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.30 | 2-Layer Sandwich | 
|   | 3.30.565 | Heat Shock Protein 90 | 
|   | 3.30.565.10 | Histidine kinase-like ATPase, C-terminal domain | 
Domain Context
CATH Clusters
| Superfamily | Histidine kinase-like ATPase, C-terminal domain | 
| Functional Family | Mitochondrial pyruvate dehydrogenase kinase isoform 2 | 
Enzyme Information
| 2.7.11.2 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase. based on mapping to UniProt Q64536 ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate. -!- Has no activating compound but is specific for its substrate. -!- A mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. -!- Phosphorylation inactivates EC 1.2.4.1. -!- Formerly EC 2.7.1.99. | 
UniProtKB Entries (2)
| Q64536 | PDK2_RAT Rattus norvegicus [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | 
| P10515 | ODP2_HUMAN Homo sapiens Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | 
PDB Structure
| PDB | 3CRK | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2. J.Biol.Chem. | 
