› 5dgm

X-ray diffraction
2.86Å resolution

Crystal structure of human FPPS in complex with monophosphonate compound 7

Released:
DOI: 10.2210/pdb5dgm/pdb
PDB entry 5dgm coloured by chain, front view.
PDB entry 5dgm coloured by chain, side view.
PDB entry 5dgm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A General Strategy for Targeting Drugs to Bone.
Jahnke W, Bold G, Marzinzik AL, Ofner S, Pellé X, Cotesta S, Bourgier E, Lehmann S, Henry C, Hemmig R, Stauffer F, Hartwieg JC, Green JR, Rondeau JM
Angew Chem Int Ed Engl 54 14575-9 (2015)
PMID: 26457482

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 59Z 1 x 59Z
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: 110.723Å b: 110.723Å c: 76.775Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.185 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Approaches for Designing new Potent Inhibitors of Farnesyl Pyrophosphate Synthase.
Rodriguez et al. (2016)
3 more