6hxh

X-ray diffraction
3.3Å resolution

Structure of the human ATP citrate lyase holoenzyme in complex with citrate, coenzyme A and Mg.ADP

Released:

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, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 1050 amino acids
Theoretical weight: 115.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53396 (Residues: 1-424, 488-1101; Coverage: 94%)
  • Best match: P53396-2 (Residues: 1-424, 478-1091)
Gene name: ACLY
Sequence domains:

Ligands and Environments


Cofactor: Ligand COA 8 x COA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 150.364Å b: 154.011Å c: 154.087Å
α: 91.53° β: 110.04° γ: 107.46°
R-values:
R R work R free
0.157 0.156 0.187
Expression system: Escherichia coli