4qoh

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<StructureSection load='4qoh' size='340' side='right'caption='[[4qoh]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4qoh' size='340' side='right'caption='[[4qoh]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qoh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QOH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QOH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qoh]] 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=4QOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QOH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qod|4qod]], [[4qoe|4qoe]], [[4qof|4qof]], [[4qog|4qog]], [[4qoi|4qoi]], [[4qoj|4qoj]]</td></tr>
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<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NQO2, NMOR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qoh OCA], [https://pdbe.org/4qoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qoh RCSB], [https://www.ebi.ac.uk/pdbsum/4qoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qoh ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.99.2 1.10.99.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qoh OCA], [http://pdbe.org/4qoh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qoh RCSB], [http://www.ebi.ac.uk/pdbsum/4qoh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qoh ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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==See Also==
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*[[Quinone reductase|Quinone reductase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Antoine, M]]
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[[Category: Antoine M]]
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[[Category: Boutin, J A]]
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[[Category: Boutin JA]]
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[[Category: Ferry, G]]
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[[Category: Ferry G]]
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[[Category: Isabet, T]]
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[[Category: Isabet T]]
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[[Category: Serriere, J]]
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[[Category: Serriere J]]
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[[Category: Fad resveratrol]]
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[[Category: Oxidoreductase]]
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[[Category: Oxidoreductase flavoprotein]]
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Current revision

Crystal structure of fad quinone reductase 2 in complex with resveratrol at 1.6A

PDB ID 4qoh

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