› 4ng6

X-ray diffraction
2.35Å resolution

The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates

Released:
DOI: 10.2210/pdb4ng6/pdb
PDB entry 4ng6 coloured by chain, front view.
PDB entry 4ng6 coloured by chain, side view.
PDB entry 4ng6 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: 43.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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:
Ligand MG 3 x MG
Ligand IPE 1 x IPE
Ligand RIS 1 x RIS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P41212
Unit cell:
a: 111.74Å b: 111.74Å c: 66.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.23
Expression system: Escherichia coli BL21

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