Structure of closed cytochrome P450 EryK

Investigating the Structural Plasticity of a Cytochrome P450: Three-Dimensional Structures of P450 Eryk and Binding to its Physiological Substrate.

CYTOCROME P450 CYP113A1, ERYTHROMYCIN B/D C-12 HYDROXYLASE

MFADVETTCCARRTLTTIDEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLRDTATFSSDPTRVIEGA
SPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEPRIRDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHE
QFGDWSGALVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLISRLVLAEVDGRALDDEEAANFSTALLL
AGHITTTVLLGNIVRTLDEHPAHWDAAAEDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNTWVLSAN
RDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENRVALEEIIARFGRLTVDRDDERLRHFEQIVLGTRHLP
VLAGSSPRQSA

2.0M AMMONIUM SULPHATE, 0.1M BIS-TRIS PH 6.5

STRUCTURE OF OPEN HISTIDINE TAGGED CYTOCHROME P450 ERYK

STRUCTURE OF THE OPEN HISTIDINE TAGGED C. SAVINO, CYTOCHROME P450 ERYK

STRUCTURE OF HISTIDINE TAGGED CYTOCHROME P450 ERYK IN COMPLEX WITH INHIBITOR CLOTRIMAZOLE (CLT)

STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX WITH INHIBITOR KETOCONAZOLE (KC)

STRUCTURE OF CYTOCHROME P450 ERYK IN COMPLEX WITH ITS NATURAL SUBSTRATE ERD

ENGINEERED RESIDUE IN CHAIN A, MET 1 TO LEU ENGINEERED RESIDUE IN CHAIN A, PHE 330 TO LEU

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. COORDINATES START FROM A.A. 17 BECAUSE THERE WAS NOT ELECTRON DENSITY FOR PREVIOUS RESIDUES

OXIDOREDUCTASE, IRON, HEME, MONOOXYGENASE, METAL-BINDING, ANTIBIOTIC BIOSYNTHESIS, TIE-ROD MECHANISM OF ACTION, CYTOCHROME P450, SUBSTRATE SPECIFICITY