2for

X-ray diffraction
2Å resolution

Crystal Structure of the Shigella flexneri Farnesyl Pyrophosphate Synthase Complex with an Isopentenyl Pyrophosphate

Released:
Source organism: Shigella flexneri
Entry authors: Minasov G, Brunzelle JS, Shuvalova L, Collart FR, Joachimiak A, Anderson WF, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Geranyltranstransferase (Farnesyldiphosphate synthase) Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 34.92 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2UXE9 (Residues: 1-299; Coverage: 100%)
Gene names: SF0358, ispA
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: APS BEAMLINE 5ID-B
Spacegroup: P61
Unit cell:
a: 75.664Å b: 75.664Å c: 216.66Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.181 0.233
Expression system: Escherichia coli BL21(DE3)