1dz6

<table><tr><td colspan='2'>[[1dz6]] is a 2 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=1DZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DZ6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cpp|2cpp]], [[3cpp|3cpp]], [[4cpp|4cpp]], [[5cpp|5cpp]], [[6cpp|6cpp]], [[7cpp|7cpp]], [[8cpp|8cpp]], [[1cp4|1cp4]], [[2cp4|2cp4]], [[3cp4|3cp4]], [[4cp4|4cp4]], [[5cp4|5cp4]], [[6cp4|6cp4]], [[1noo|1noo]], [[1pha|1pha]], [[1phb|1phb]], [[1phc|1phc]], [[1phd|1phd]], [[1phe|1phe]], [[1phf|1phf]], [[1phg|1phg]], [[1akd|1akd]], [[1dz4|1dz4]], [[1dz8|1dz8]], [[1dz9|1dz9]]</div></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=1dz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz6 OCA], [http://pdbe.org/1dz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dz6 RCSB], [http://www.ebi.ac.uk/pdbsum/1dz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz6 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 ==

Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.

The catalytic pathway of cytochrome p450cam at atomic resolution.,Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG Science. 2000 Mar 3;287(5458):1615-22. PMID:10698731<ref>PMID:10698731</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 1dz6" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus fluorescens putidus flugge 1886]]

[[Category: Benson, D E]]

[[Category: Berendzen, J]]

[[Category: Chu, K]]

[[Category: Maves, S A]]

[[Category: Petsko, G A]]

[[Category: Ringe, D]]

[[Category: Schlichting, I]]

[[Category: Sligar, S G]]

[[Category: Stock, A M]]

[[Category: Sweet, R M]]

[[Category: Oxidoreductase]]