CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.970 | Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.970 |
| Functional Family | Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial |
Enzyme Information
| 1.2.4.1 |
Pyruvate dehydrogenase (acetyl-transferring).
based on mapping to UniProt P08559
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
-!- It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
|
UniProtKB Entries (1)
| P08559 |
ODPA_HUMAN
Homo sapiens
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
|
PDB Structure
| PDB | 3EXG |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
Structure
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