4XE3

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

Summary for 4XE3

Entry DOI	10.2210/pdb4xe3/pdb
Descriptor	Cytochrome P-450, PROTOPORPHYRIN IX CONTAINING FE, 1-[(2-CHLOROPHENYL)(DIPHENYL)METHYL]-1H-IMIDAZOLE, ... (5 entities in total)
Functional Keywords	p450, clotrimazole, epoxidase, oleandomycin, oxidoreductase
Biological source	Streptomyces antibioticus
Total number of polymer chains	2
Total formula weight	92907.42
Authors	Montemiglio, L.C.,Parisi, G.,Scaglione, A.,Savino, C.,Vallone, B. (deposition date: 2014-12-22, release date: 2015-11-04, Last modification date: 2023-09-27)
Primary citation	Montemiglio, L.C.,Parisi, G.,Scaglione, A.,Sciara, G.,Savino, C.,Vallone, B. Functional analysis and crystallographic structure of clotrimazole bound OleP, a cytochrome P450 epoxidase from Streptomyces antibioticus involved in oleandomycin biosynthesis. Biochim.Biophys.Acta, 1860:465-475, 2015 Cited by PubMed Abstract: OleP is a cyt P450 from Streptomyces antibioticus carrying out epoxigenation of the antibiotic oleandomycin during its biosynthesis. The timing of its reaction has not been fully clarified, doubts remain regarding its substrate and catalytic mechanism. PubMed: 26475642 DOI: 10.1016/j.bbagen.2015.10.009 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.65 Å)

Structure validation