4xqr

X-ray diffraction
2.15Å resolution

Crystal structure of unliganded human FPPS at 2.15 angstrom resolution

Released:
Source organism: Homo sapiens
Entry authors: Park J, Berghuis AM

Function and Biology Details

Reactions catalysed:
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl pyrophosphate synthase Chain: F
Molecule details ›
Chain: F
Length: 375 amino acids
Theoretical weight: 43.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14324 (Residues: 67-419; Coverage: 84%)
  • Best match: P14324-2 (Residues: 1-353)
Gene names: FDPS, FPS, KIAA1293
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P41212
Unit cell:
a: 110.85Å b: 110.85Å c: 78.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.225
Expression system: Escherichia coli