PDBe 3cp6

X-ray diffraction
1.95Å resolution

Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor

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

Function and Biology Details

Reactions catalysed:
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl 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: 376 amino acids
Theoretical weight: 43.25 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: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 112.531Å b: 112.531Å c: 62.919Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.243
Expression system: Escherichia coli BL21(DE3)