› 4xe3

X-ray diffraction
2.65Å resolution

OleP, the cytochrome P450 epoxidase from Streptomyces antibioticus involved in Oleandomycin biosynthesis: functional analysis and crystallographic structure in complex with clotrimazole.

Released:
DOI: 10.2210/pdb4xe3/pdb
PDB entry 4xe3 coloured by chain, front view.
PDB entry 4xe3 coloured by chain, side view.
PDB entry 4xe3 coloured by chain, top view.
Source organism: Streptomyces antibioticus
Primary publication:
Functional analysis and crystallographic structure of clotrimazole bound OleP, a cytochrome P450 epoxidase from Streptomyces antibioticus involved in oleandomycin biosynthesis.
Montemiglio LC, Parisi G, Scaglione A, Sciara G, Savino C, Vallone B
Biochim Biophys Acta 1860 465-75 (2016)
PMID: 26475642

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176826 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P-450 Chains: A, B
Molecule details ›
Chains: A, B
Length: 407 amino acids
Theoretical weight: 45.01 KDa
Source organism: Streptomyces antibioticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q59819 (Residues: 1-407; Coverage: 100%)
Gene name: oleP
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

3 bound ligands:
Ligand HEM 2 x HEM
Ligand CL6 2 x CL6
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 115.937Å b: 117.379Å c: 174.664Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.26
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Recent trends in biocatalysis.
Yi et al. (2021)
2 more

5 mentions without citation

Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
Rudolf et al. (2017)
4 more