PDBe 5te1

X-ray diffraction
2.25Å resolution

C20S, C293G Mutant N-terminal Human ATP Citrate Lyase Bound to 4R-Hydroxycitrate

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-citrate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 828 amino acids
Theoretical weight: 90.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53396 (Residues: 1-817; Coverage: 74%)
Gene name: ACLY
Sequence domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 98.77Å b: 73.32Å c: 131.37Å
α: 90° β: 97.06° γ: 90°
R-values:
R R work R free
0.191 0.188 0.247
Expression system: Escherichia coli