PDBe 3exf

X-ray diffraction
3Å resolution

Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex

Released:

Function and Biology Details

Reaction catalysed:
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). 

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 329 amino acids
Theoretical weight: 35.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11177 (Residues: 31-359; Coverage: 92%)
Gene names: PDHB, PHE1B
Sequence domains:
Structure domains:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 382 amino acids
Theoretical weight: 42.55 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

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 103.389Å b: 129.668Å c: 144.946Å
α: 90° β: 109.15° γ: 90°
R-values:
R R work R free
0.189 0.185 0.263
Expression system: Escherichia coli