6uuz

Electron Microscopy
3Å resolution

Structure of ACLY in the presence of citrate and CoA

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-20903

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: 1100 amino acids
Theoretical weight: 120.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P53396 (Residues: 1-1100; Coverage: 100%)
Gene name: ACLY
Sequence domains:

Ligands and Environments


Cofactor: Ligand COA 4 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution:
Relevant EMDB volumes: EMD-20903
Expression system: Escherichia coli BL21