› 2g28

X-ray diffraction
1.85Å 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142723 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate dehydrogenase E1 component Chains: A, B
Molecule details ›
Chains: A, B
Length: 886 amino acids
Theoretical weight: 99.66 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AFG8 (Residues: 2-887; Coverage: 100%)
Gene names: JW0110, aceE, b0114
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TDK 2 x TDK
1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 81.99Å b: 143.2Å c: 82.53Å
α: 90° β: 102.61° γ: 90°
R-values:
R R work R free
0.227 0.216 0.24
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The pyruvate dehydrogenase complexes: structure-based function and regulation.
Patel et al. (2014)
9 more

1 mention without citation

Rules governing selective protein carbonylation.
Maisonneuve et al. (2009)