2opn

X-ray diffraction
2.7Å resolution

Human Farnesyl Diphosphate Synthase Complexed with Bisphosphonate BPH-527

Released:
Source organism: Homo sapiens
Entry authors: Cao R, Gao YG, Robinson H, Goddard A, Oldfield E

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-146902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl pyrophosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 43.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14324 (Residues: 67-419; Coverage: 84%)
Gene names: FDPS, FPS, KIAA1293
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P41212
Unit cell:
a: 111.652Å b: 111.652Å c: 66.841Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.272 0.272 0.298
Expression system: Escherichia coli BL21(DE3)