6ui9

Electron Microscopy
3.1Å resolution

Structure of human ATP citrate lyase in complex with acetyl-CoA and oxaloacetate

Released:
Source organism: Homo sapiens
Primary publication:
Molecular basis for acetyl-CoA production by ATP-citrate lyase.
Nat. Struct. Mol. Biol. (2019)
PMID: 31873304
Related structures: EMD-20783

Function and Biology Details

Reaction catalysed:
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-citrate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1101 amino acids
Theoretical weight: 120.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53396 (Residues: 1-1101; Coverage: 100%)
Gene name: ACLY
Sequence domains:

Ligands and Environments


Cofactor: Ligand ACO 4 x ACO
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-20783
Expression system: Escherichia coli