› 6n7z

X-ray diffraction
2.55Å resolution

Crystal structure of human FPPS in complex with an allosteric inhibitor YF-02037

Released:
DOI: 10.2210/pdb6n7z/pdb
Model geometry
Data not analysed
Fit model/data
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PDB entry 6n7z coloured by chain, front view.
PDB entry 6n7z coloured by chain, side view.
PDB entry 6n7z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chirality-Driven Mode of Binding of α-Aminophosphonic Acid-Based Allosteric Inhibitors of the Human Farnesyl Pyrophosphate Synthase (hFPPS).
Feng Y, Park J, Li SG, Boutin R, Viereck P, Schilling MA, Berghuis AM, Tsantrizos YS
J Med Chem 62 9691-9702 (2019)
PMID: 31577901

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: 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

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand KF7 1 x KF7
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BRUKER METALJET
Spacegroup: P41212
Unit cell:
a: 110.862Å b: 110.862Å c: 75.038Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.232 0.281
Expression system: Escherichia coli

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Citations

1 review citation

Phosphonate and Bisphosphonate Inhibitors of Farnesyl Pyrophosphate Synthases: A Structure-Guided Perspective.
Park et al. (2020)
1 other article

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