PDBe 1fyc

Solution NMR

INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX, NMR, 1 STRUCTURE

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: 106 amino acids
Theoretical weight: 11.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10515 (Residues: 214-315; Coverage: 16%)
Gene names: DLAT, DLTA
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

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli