4kk2

X-ray diffraction
2.2Å resolution

Crystal structure of a chimeric FPP/GFPP synthase (TARGET EFI-502313c) from Artemisia spiciformiS (1-72:GI751454468,73-346:GI75233326), apo structure

Released:
Source organism: Artemisia spiciformis
Entry authors: Vetting MW, Toro R, Bhosle R, Al Obaidi NF, Washington E, Scott Glenn A, Chowdhury S, Evans B, Hammonds J, Hillerich B, Love J, Seidel RD, Imker HJ, Poulter CD, Gerlt JA, Almo SC, Enzyme Function Initiative (EFI)

Function and Biology Details

Reactions catalysed:
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
2 prenyl diphosphate = diphosphate + chrysanthemyl diphosphate
2 prenyl diphosphate = diphosphate + lavandulyl diphosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-182195 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl diphosphate synthase 1; Monoterpene synthase FDS-5, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 42.15 KDa
Source organism: Artemisia spiciformis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7XYS8 (Residues: 50-120; Coverage: 18%)
  • Canonical: Q7XYS9 (Residues: 73-346; Coverage: 79%)
Gene names: FDS-1, FDS-5
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P61
Unit cell:
a: 122.145Å b: 122.145Å c: 114.282Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.157 0.198
Expression system: Escherichia coli BL21(DE3)