› 4kq5

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb4kq5/pdb
PDB entry 4kq5 coloured by chain, front view.
PDB entry 4kq5 coloured by chain, side view.
PDB entry 4kq5 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Barnett BL, Tsoumpra MK, Muniz JRC

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: 43.05 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 MG 3 x MG
Ligand ZOL 1 x ZOL
Ligand EDO 1 x EDO
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)

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