4kq5

X-ray diffraction
2.4Å resolution

Crystal Structure of Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate

Released:
Source organism: Homo sapiens
Entry authors: Barnett BL, Tsoumpra MK, Muniz JRC

Function and Biology Details

Reactions catalysed:
Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl 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: 43.05 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: RIGAKU MICROMAX-007 HF
Spacegroup: P41212
Unit cell:
a: 111.65Å b: 111.65Å c: 67.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.247
Expression system: Escherichia coli BL21(DE3)