› 6ofv

X-ray diffraction
1.91Å resolution

Function and Biology Details

Reaction catalysed: 
(2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-575518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epi-isozizaene synthase Chain: A
Molecule details ›
Chain: A
Length: 381 amino acids
Theoretical weight: 43.6 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9K499 (Residues: 1-361; Coverage: 100%)
Gene names: SC7E4.19, SCO5222, cyc1
Sequence domains: Terpene synthase family 2, C-terminal metal binding

Ligands and Environments

5 bound ligands:
Ligand POP 1 x POP
Ligand MG 3 x MG
Ligand BTM 1 x BTM
Ligand GOL 3 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 53.25Å b: 47.09Å c: 75.59Å
α: 90° β: 95.13° γ: 90°
R-values:
R R work R free
0.158 0.155 0.202
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Structure, catalysis, and inhibition mechanism of prenyltransferase.
Chang et al. (2021)
2 more

1 mention without citation

Crystal structure of F95Q epi-isozizaene synthase, an engineered sesquiterpene cyclase that generates biofuel precursors β- and γ-curcumene.
Blank et al. (2019)