1p2y

<table><tr><td colspan='2'>[[1p2y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P2Y FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NCT:(S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE'>NCT</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAMC OR CYP101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2y OCA], [http://pdbe.org/1p2y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p2y RCSB], [http://www.ebi.ac.uk/pdbsum/1p2y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2y ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system.

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== Publication Abstract from PubMed ==

Crystallographic and spectroscopic studies have been undertaken to characterize the binding behavior of the non-native substrate nicotine in the active site of the monooxygenase hemoprotein cytochrome P450cam. Despite the existence of a theoretical model that is consistent with the observed distribution of monooxygenation products, the crystal structure of the complex indicates that the primary binding mode of nicotine is unproductive. The structure is confirmed by spectral data that indicate direct coordination of substrate pyridine nitrogen with the heme iron. This would be the proper structure for evaluating binding affinity and inhibition. Reduction of the heme from Fe(III) to Fe(II) and introduction of carbon monoxide into crystals of the nicotine-P450cam complex, to simulate molecular oxygen binding, produces reorientation of the nicotine. This orientation is the appropriate one for predicting regioselectivity and the kinetic features of substrate oxidation. While it is not clear that such complicated behavior will be exhibited for other enzyme-substrate interactions, it is clear that a single crystal structure for a given substrate-enzyme interaction may not provide a good description of the binding mode responsible for product formation.

Crystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101).,Strickler M, Goldstein BM, Maxfield K, Shireman L, Kim G, Matteson DS, Jones JP Biochemistry. 2003 Oct 21;42(41):11943-50. PMID:14556625<ref>PMID:14556625</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1p2y" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus fluorescens putidus flugge 1886]]

[[Category: Camphor 5-monooxygenase]]

[[Category: Goldstein, B M]]

[[Category: Jones, J P]]

[[Category: Kim, G]]

[[Category: Matteson, D]]

[[Category: Maxfield, K]]

[[Category: Shireman, L]]

[[Category: Strickler, M]]

[[Category: Oxidoreductase]]