› 4n9u

X-ray diffraction
2.11Å resolution

The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates

Released:
DOI: 10.2210/pdb4n9u/pdb
PDB entry 4n9u coloured by chain, front view.
PDB entry 4n9u coloured by chain, side view.
PDB entry 4n9u coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Tsoumpra MK, Muniz JRC, Barnett BL, Pilka E, Kwaasi AA, Kavanagh KL, Evdokimov A, Walter RL, Ebetino FH, 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: 43.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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 RIS 1 x RIS
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P41212
Unit cell:
a: 111.11Å b: 111.11Å c: 69.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.24
Expression system: Escherichia coli BL21

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