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3g5m

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==Synthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory activity==
==Synthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory activity==
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<StructureSection load='3g5m' size='340' side='right' caption='[[3g5m]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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<StructureSection load='3g5m' size='340' side='right'caption='[[3g5m]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3g5m]] 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=3G5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G5M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3g5m]] 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=3G5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G5M 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=XM5:6-METHOXY-9-METHYL[1,3]DIOXOLO[4,5-H]QUINOLIN-8(9H)-ONE'>XM5</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]] 1.84&#8491;</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='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=XM5:6-METHOXY-9-METHYL[1,3]DIOXOLO[4,5-H]QUINOLIN-8(9H)-ONE'>XM5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3g5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5m OCA], [https://pdbe.org/3g5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g5m RCSB], [https://www.ebi.ac.uk/pdbsum/3g5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g5m ProSAT]</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=3g5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5m OCA], [http://pdbe.org/3g5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g5m RCSB], [http://www.ebi.ac.uk/pdbsum/3g5m PDBsum]</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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/3g5m_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/3g5m_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Cushman, M]]
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[[Category: Large Structures]]
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[[Category: Maiti, A]]
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[[Category: Cushman M]]
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[[Category: Marler, L]]
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[[Category: Maiti A]]
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[[Category: Mesecar, A D]]
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[[Category: Marler L]]
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[[Category: Pegan, S D]]
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[[Category: Mesecar AD]]
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[[Category: Pezzuto, J M]]
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[[Category: Pegan SD]]
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[[Category: Sturdy, M]]
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[[Category: Pezzuto JM]]
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[[Category: Casimiroin]]
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[[Category: Sturdy M]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Metal-binding]]
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[[Category: Nq02]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphoprotein]]
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[[Category: Qr2]]
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Current revision

Synthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory activity

PDB ID 3g5m

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