PDBe 5tes

X-ray diffraction
2.4Å resolution

TEV Cleaved Human ATP Citrate Lyase Bound to Citrate and ADP

Released:
Source organism: Homo sapiens
Primary publication:
Binding of hydroxycitrate to human ATP-citrate lyase.
Acta Crystallogr D Struct Biol 73 660-671 (2017)
PMID: 28777081

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-citrate synthase Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 47.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53396 (Residues: 1-425; Coverage: 39%)
Gene name: ACLY
Sequence domains: ATP citrate lyase citrate-binding
ATP-citrate synthase Chain: B
Molecule details ›
Chain: B
Length: 324 amino acids
Theoretical weight: 35.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53396 (Residues: 487-810; Coverage: 29%)
Gene name: ACLY
Sequence domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 56.17Å b: 85.14Å c: 199.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.252
Expression system: Escherichia coli