Function and Biology Details
Reaction catalysed:
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
- not assigned
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 106 amino acids
Theoretical weight: 11.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P10515 (Residues: 214-315; Coverage: 16%)
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
simulated annealing
Expression system: Escherichia coli
