› 3n5h

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl pyrophosphate synthase Chain: F
Molecule details ›
Chain: F
Length: 350 amino acids
Theoretical weight: 40.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14324 (Residues: 72-419; Coverage: 83%)
Gene names: FDPS, FPS, KIAA1293
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:
Ligand GO0 2 x GO0
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P41212
Unit cell:
a: 111.062Å b: 111.062Å c: 78.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.223 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Biochemical and molecular mechanisms of action of bisphosphonates.
Rogers et al. (2011)
24 more

3 mentions without citation

A novel small-molecule compound targeting CD147 inhibits the motility and invasion of hepatocellular carcinoma cells.
Fu et al. (2016)
2 more