PDBe 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:
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:
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (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%)
  • Best match: P14324-2 (Residues: 1-353)
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: 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)