› 4q23

X-ray diffraction
1.98Å resolution

The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates

Released:
DOI: 10.2210/pdb4q23/pdb
PDB entry 4q23 coloured by chain, front view.
PDB entry 4q23 coloured by chain, side view.
PDB entry 4q23 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Tsoumpra MK, Muniz JRC, Barnett BL, Kwaasi AA, Pilka ES, Kavanagh KL, Evdokimov A, Walter RL, Ebetino FH, von Delft F, Oppermann U, Russell RGG, Dunford JE

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: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 43.11 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:
Ligand RIS 1 x RIS
Ligand MG 3 x MG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P41212
Unit cell:
a: 111.36Å b: 111.36Å c: 67.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.223
Expression system: Escherichia coli BL21(DE3)

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