› 7rkz

Electron Microscopy
2.6Å resolution

Structure of ACLY D1026A-substrates-asym-int

Released:
DOI: 10.2210/pdb7rkz/pdb
PDB entry 7rkz coloured by chain, front view.
PDB entry 7rkz coloured by chain, side view.
PDB entry 7rkz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Allosteric role of the citrate synthase homology domain of ATP citrate lyase.
Wei X, Schultz K, Pepper HL, Megill E, Vogt A, Snyder NW, Marmorstein R
OpenAccess logo Nat Commun 14 2247 (2023)
PMID: 37076498
Related structures: EMD-24511

Function and Biology Details

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

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: 120.94 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 COA 4 x COA
4 bound ligands:
Ligand ADP 3 x ADP
Ligand Q5B 3 x Q5B
Ligand FLC 4 x FLC
Ligand UNL 2 x UNL
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.6Å
Relevant EMDB volumes: EMD-24511
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Allosteric role of the citrate synthase homology domain of ATP citrate lyase.
Wei et al. (2023)