› 3pff

X-ray diffraction
2.3Å resolution

Truncated human atp-citrate lyase with ADP and tartrate bound

Released:
DOI: 10.2210/pdb3pff/pdb
PDB entry 3pff coloured by chain, front view.
PDB entry 3pff coloured by chain, side view.
PDB entry 3pff coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.
Sun T, Hayakawa K, Fraser ME
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1168-72 (2011)
PMID: 22102020

Function and Biology Details

Reaction catalysed: 
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-156797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-citrate synthase Chain: A
Molecule details ›
Chain: A
Length: 829 amino acids
Theoretical weight: 90.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53396 (Residues: 1-817; Coverage: 74%)
Gene name: ACLY
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand TLA 1 x TLA
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 167.54Å b: 61.7Å c: 107.98Å
α: 90° β: 125.47° γ: 90°
R-values:
R R work R free
0.171 0.168 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

ATP-citrate lyase: genetics, molecular biology and therapeutic target for dyslipidemia.
Burke et al. (2017)
2 more

4 mentions without citation

A defect in ATP-citrate lyase links acetyl-CoA production, virulence factor elaboration and virulence in Cryptococcus neoformans.
Griffiths et al. (2012)
3 more