View source for 3nv6


==Crystal Structure of Camphor-Bound CYP101D2==
<StructureSection load='3nv6' size='340' side='right'caption='[[3nv6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nv6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Novosphingobium_aromaticivorans_DSM_12444 Novosphingobium aromaticivorans DSM 12444]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NV6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nv6 OCA], [https://pdbe.org/3nv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nv6 RCSB], [https://www.ebi.ac.uk/pdbsum/3nv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nv6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2G8A2_NOVAD Q2G8A2_NOVAD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CYP101D2 from Novosphingobium aromaticivorans DSM12444 is closely related to CYP101D1 from the same bacterium and to P450cam (CYP101A1) from Pseudomonas putida. All three are capable of oxidising camphor stereoselectively to 5-exo-hydroxycamphor. The crystal structure of CYP101D2 reveals that the likely ferredoxin binding site on the proximal face is largely positively charged, similar to that of CYP101D1. However, both the native and camphor-soaked forms of CYP101D2 have open conformations with an access channel. In the active site of the camphor-soaked form the camphor carbonyl interacts with the heme iron-bound water. Two other potential camphor binding sites were also identified from electron densities in the camphor-soaked structure: one is located in the access channel, flanked by the B/C and F/G loops and the I helix, and the other in a cavity on the surface of the enzyme near the F helix side of the F/G loop. The observed open structures may be conformers of the CYP101D2 enzyme which enable the substrate to enter the buried active site via a conformational selection mechanism. The second and third binding sites may be intermediate locations of substrate entry and translocation into the active site, and provide insight into a multi-step substrate binding mechanism.

The structure of CYP101D2 unveils a potential path for substrate entry into the active site.,Yang W, Bell SG, Wang H, Zhou W, Bartlam M, Wong LL, Rao Z Biochem J. 2010 Oct 15. PMID:20950270<ref>PMID:20950270</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3nv6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Novosphingobium aromaticivorans DSM 12444]]
[[Category: Bartlam M]]
[[Category: Bell SG]]
[[Category: Rao Z]]
[[Category: Wang H]]
[[Category: Wong LL]]
[[Category: Yang W]]
[[Category: Zhou WH]]