› 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 4rxa coloured by chain and viewed from the front.
PDB 4rxa coloured by chain and viewed from the side.
PDB 4rxa coloured by chain and viewed from the top.
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: 
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

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: 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)