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:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 8.38 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 80 amino acids
Theoretical weight: 8.38 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P06959 (Residues: 206-284; Coverage: 13%)
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:
XPLOR
Expression system: Escherichia coli BL21(DE3)
