› 2ozl

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140174 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial Chains: A, C
Molecule details ›
Chains: A, C
Length: 365 amino acids
Theoretical weight: 40.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08559 (Residues: 30-390; Coverage: 93%)
Gene names: PDHA1, PHE1A
Sequence domains: Dehydrogenase E1 component
Structure domains: Rossmann fold
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Chains: B, D
Molecule details ›
Chains: B, D
Length: 341 amino acids
Theoretical weight: 37.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11177 (Residues: 32-359; Coverage: 91%)
Gene names: PDHB, PHE1B
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 2 x TPP
2 bound ligands:
Ligand MG 2 x MG
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 64.9Å b: 126.4Å c: 190.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.221
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Regulation of pyruvate metabolism and human disease.
Gray et al. (2014)
4 more

3 mentions without citation

Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
Kato et al. (2008)
2 more