The structure of CYP101D2 unveils a potential path for substrate entry into the active site

Biochemical Journal

Volumn 433, Issue 1, 2011, Pages 85-93

  Yang, Wen ^a   Bell, Stephen G ^b   Wang, Hui ^c   Zhou, Weihong ^a   Bartlam, Mark ^a   Wong, Luet Lok ^b   Rao, Zihe ^a,c  

^a NANKAI UNIVERSITY   (China)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c TSINGHUA UNIVERSITY   (China)

Author keywords

Access channel; Crystal structure; Cytochrome P450; Multi step binding mechanism; Novosphingobium aromaticivorans DSM12444; Open conformation

Indexed keywords

CAMPHOR; CARBONYL DERIVATIVE; CYTOCHROME P450; CYTOCHROME P450 101D1; CYTOCHROME P450 101D2; FERREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRON; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME LOCALIZATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

BACTERIAL PROTEINS; BINDING SITES; CAMPHOR; CAMPHOR 5-MONOOXYGENASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; OXYGEN; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); DRYOBALANOPS; NOVOSPHINGOBIUM AROMATICIVORANS; PSEUDOMONAS PUTIDA;

EID: 79551473016     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101017     Document Type: Article

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