› 3lq2

X-ray diffraction
1.96Å resolution

Function and Biology Details

Reaction catalysed: 
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142724 (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: 99.6 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AFG9 (Residues: 2-887; Coverage: 100%)
Gene names: ECs0118, Z0124, aceE
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 2 x TPP
3 bound ligands:
Ligand MG 2 x MG
Ligand PO4 2 x PO4
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 80.65Å b: 141.77Å c: 83.42Å
α: 90° β: 103.36° γ: 90°
R-values:
R R work R free
0.194 0.194 0.223
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for a "direct pathway" between the 4'-aminopyrimidine N1' atoms.
Nemeria et al. (2010)
1 more