› 7lla

Electron Microscopy
2.97Å resolution

Structure of human ATP citrate lyase in complex with acetyl-CoA and oxaloacetate (EM map was generated in Cryosparc with non-uniform refinement)

Released:
DOI: 10.2210/pdb7lla/pdb
PDB entry 7lla coloured by chain, front view.
PDB entry 7lla coloured by chain, side view.
PDB entry 7lla coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Reply to: Acetyl-CoA is produced by the citrate synthase homology module of ATP-citrate lyase.
Wei X, Marmorstein R
Nat Struct Mol Biol 28 639-641 (2021)
PMID: 34294921
Related structures: EMD-23413

Function and Biology Details

Reaction catalysed: 
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-547143 (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:
Ligand OAA 8 x OAA
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.97Å
Relevant EMDB volumes: EMD-23413
Expression system: Escherichia coli BL21

Quick links

Citations

1 citations in other articles

The structure of succinyl-CoA synthetase bound to the succinyl-phosphate intermediate clarifies the catalytic mechanism of ATP-citrate lyase.
Huang et al. (2022)