› 5djv

X-ray diffraction
2.3Å 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-537544 (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

1 bound ligand:
Ligand 5BL 1 x 5BL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 111.88Å b: 111.88Å c: 74.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.209 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Biophysics in drug discovery: impact, challenges and opportunities.
Renaud et al. (2016)
6 more