› 4rxa

X-ray diffraction
2.2Å resolution

Crystal structure of human farnesyl diphosphate synthase in complex with BPH-1358

Released:
DOI: 10.2210/pdb4rxa/pdb
PDB entry 4rxa coloured by chain, front view.
PDB entry 4rxa coloured by chain, side view.
PDB entry 4rxa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Farnesyl diphosphate synthase inhibitors with unique ligand-binding geometries.
Liu YL, Cao R, Wang Y, Oldfield E
ACS Med Chem Lett 6 349-54 (2015)
PMID: 25815158

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: 348 amino acids
Theoretical weight: 40.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14324 (Residues: 72-419; Coverage: 83%)
Gene names: FDPS, FPS, KIAA1293
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:
Ligand 3F2 1 x 3F2
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P41212
Unit cell:
a: 110.757Å b: 110.757Å c: 77.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.221 0.263
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Targeting Small GTPases and Their Prenylation in Diabetes Mellitus.
Gendaszewska-Darmach et al. (2021)
2 more

1 mention without citation

Farnesyl diphosphate synthase inhibitors with unique ligand-binding geometries.
Liu et al. (2015)