Function and Biology Details
Reaction catalysed:
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo 60-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Molecule details ›
Chains: A, B, C, D, E
Length: 242 amino acids
Theoretical weight: 26.44 KDa
Source organism: Geobacillus stearothermophilus
UniProt:
Sequence domains: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
Length: 242 amino acids
Theoretical weight: 26.44 KDa
Source organism: Geobacillus stearothermophilus
UniProt:
- Canonical:
P11961 (Residues: 185-426; Coverage: 57%)
Sequence domains: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
CHESS BEAMLINE F1
Spacegroup:
F4132
