PDBe 3mwe

X-ray diffraction
2.2Å resolution

Truncated Human ATP-Citrate Lyase with Tartrate 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: 47.04 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: 335 amino acids
Theoretical weight: 36.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53396 (Residues: 487-821; Coverage: 30%)
Gene name: ACLY
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 168.191Å b: 60.793Å c: 109.176Å
α: 90° β: 124.96° γ: 90°
R-values:
R R work R free
0.182 0.179 0.228
Expression system: Escherichia coli BL21(DE3)