PDBe 3mwd

X-ray diffraction
2.1Å resolution

Truncated Human ATP-Citrate Lyase with Citrate Bound

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-citrate synthase Chain: A
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53396 (Residues: 1-425; Coverage: 39%)
Gene name: ACLY
Sequence domains: ATP citrate lyase citrate-binding
Structure domains:
ATP-citrate synthase Chain: B
Molecule details ›
Chain: B
Length: 334 amino acids
Theoretical weight: 36.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53396 (Residues: 487-820; Coverage: 30%)
Gene name: ACLY
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 169.197Å b: 61.704Å c: 109.421Å
α: 90° β: 125° γ: 90°
R-values:
R R work R free
0.194 0.191 0.229
Expression system: Escherichia coli BL21(DE3)