1rqj

X-ray diffraction
1.95Å resolution

Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Risedronate

Released:

Function and Biology Details

Reaction catalysed:
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-149843 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl diphosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 32.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P22939 (Residues: 1-299; Coverage: 100%)
Gene names: JW0411, b0421, ispA
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P4122
Unit cell:
a: 88.8Å b: 88.8Å c: 174.988Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.206 0.239
Expression system: Escherichia coli