PDBe 3b8k

Electron Microscopy
8.8Å resolution

Structure of the Truncated Human Dihydrolipoyl Acetyltransferase (E2)

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 239 amino acids
Theoretical weight: 25.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10515 (Residues: 409-647; Coverage: 37%)
Gene names: DLAT, DLTA
Sequence domains: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 8.8Å
Relevant EMDB volumes: EMD-1448
Expression system: Escherichia coli BL21(DE3)