3b7l

X-ray diffraction
1.95Å resolution

Human farnesyl diphosphate synthase complexed with MG and minodronate

Released:
Source organism: Homo sapiens
Entry authors: Pilka ES, Dunford JE, Guo K, Pike ACW, Kavanagh KL, von Delft F, Ebetino FH, Arrowsmith CH, Edwards AM, Russell RGG, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reactions catalysed:
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-146902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl pyrophosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 356 amino acids
Theoretical weight: 40.9 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P41212
Unit cell:
a: 110.922Å b: 110.922Å c: 67.308Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.202
Expression system: Escherichia coli BL21(DE3)