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<StructureSection load='3nhr' size='340' side='right'caption='[[3nhr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3nhr' size='340' side='right'caption='[[3nhr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3nhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3nhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=RZW:5,6,8-TRIMETHOXY-1,4-DIMETHYLQUINOLIN-2(1H)-ONE'>RZW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=RZW:5,6,8-TRIMETHOXY-1,4-DIMETHYLQUINOLIN-2(1H)-ONE'>RZW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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;'>[[3nhf|3nhf]], [[3nhj|3nhj]], [[3nhk|3nhk]], [[3nhl|3nhl]], [[3nhp|3nhp]], [[3nhs|3nhs]], [[3nhu|3nhu]], [[3nhw|3nhw]], [[3nhy|3nhy]], [[3gam|3gam]], [[3g5m|3g5m]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NQO2, NMOR2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.99.2 1.10.99.2] </span></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=3nhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhr OCA], [https://pdbe.org/3nhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhr RCSB], [https://www.ebi.ac.uk/pdbsum/3nhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhr ProSAT]</span></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=3nhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhr OCA], [https://pdbe.org/3nhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhr RCSB], [https://www.ebi.ac.uk/pdbsum/3nhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN]] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref> 
[https://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An efficient method has been developed to synthesize casimiroin (1), a component of the edible fruit of Casimiroa edulis, on a multigram scale in good overall yield. The route was versatile enough to provide an array of compound 1 analogues that were evaluated as QR2 and aromatase inhibitors. In addition, X-ray crystallography studies of QR2 in complex with compound 1 and one of its more potent analogues has provided insight into the mechanism of action of this new series of QR2 inhibitors. The initial biological investigations suggest that compound 1 and its analogues merit further investigation as potential chemopreventive or chemotherapeutic agents.
 
Synthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory Activities.,Maiti A, Reddy PV, Sturdy M, Marler L, Pegan SD, Mesecar AD, Pezzuto JM, Cushman M J Med Chem. 2009 Mar 6. PMID:19265439<ref>PMID:19265439</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3nhr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sturdy, M]]
[[Category: Sturdy M]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Protein dimer]]

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