› 2ps7

X-ray diffraction
2.35Å resolution

Function and Biology Details

Reaction catalysed: 
(2E,6E)-farnesyl diphosphate = trichodiene + 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-146631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trichodiene synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 44.03 KDa
Source organism: Fusarium sporotrichioides
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13513 (Residues: 1-374; Coverage: 100%)
Gene names: TOX 5, TRI5
Sequence domains: Trichodiene synthase (TRI5)
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P3121
Unit cell:
a: 122.431Å b: 122.431Å c: 151.289Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.233 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Terpenoid synthase structures: a so far incomplete view of complex catalysis.
Gao et al. (2012)
5 more

1 mention without citation

Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2+B motif.
Vedula et al. (2008)