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 27 33-41 (2020)
PMID: 31873304
Related structures: EMD-20783

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156801 (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 BL21
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 BL21