› 3zmb

X-ray diffraction
1.9Å resolution

Native structure of Farnesyl Pyrophosphate Synthase from Pseudomonas aeruginosa PA01, with bound fragment SPB02696.

Released:
DOI: 10.2210/pdb3zmb/pdb
PDB entry 3zmb coloured by chain, front view.
PDB entry 3zmb coloured by chain, side view.
PDB entry 3zmb coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural characterization of substrate and inhibitor binding to farnesyl pyrophosphate synthase from Pseudomonas aeruginosa.
Schmidberger JW, Schnell R, Schneider G
Acta Crystallogr D Biol Crystallogr 71 721-31 (2015)
PMID: 25760619

Function and Biology Details

Reaction catalysed: 
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-191082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Geranyltranstransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 31.59 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9HWY4 (Residues: 1-295; Coverage: 100%)
Gene names: PA4043, ispA
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

3 bound ligands:
Ligand 6H6 3 x 6H6
Ligand DMS 1 x DMS
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 85.56Å b: 98.84Å c: 131.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.241
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Phosphonate and Bisphosphonate Inhibitors of Farnesyl Pyrophosphate Synthases: A Structure-Guided Perspective.
Park et al. (2020)
8 other articles

1 mention without citation

Structural characterization of substrate and inhibitor binding to farnesyl pyrophosphate synthase from Pseudomonas aeruginosa.
Schmidberger et al. (2015)