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1d4a

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[[Image:1d4a.png|left|200px]]
 
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{{STRUCTURE_1d4a| PDB=1d4a | SCENE= }}
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==CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION==
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<StructureSection load='1d4a' size='340' side='right'caption='[[1d4a]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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===CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d4a]] is a 4 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=1D4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D4A FirstGlance]. <br>
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{{ABSTRACT_PUBMED_10706635}}
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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]] 1.7&#8491;</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></td></tr>
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==About this Structure==
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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=1d4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4a OCA], [https://pdbe.org/1d4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d4a RCSB], [https://www.ebi.ac.uk/pdbsum/1d4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d4a ProSAT]</span></td></tr>
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[[1d4a]] is a 4 chain structure of [[Quinone reductase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4A OCA].
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NQO1_HUMAN NQO1_HUMAN] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/1d4a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d4a ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[NADH quinone oxidoreductase (NQO1) with inhibitor dicoumarol|NADH quinone oxidoreductase (NQO1) with inhibitor dicoumarol]]
 
*[[Quinone reductase|Quinone reductase]]
*[[Quinone reductase|Quinone reductase]]
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*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
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==Reference==
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__TOC__
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<ref group="xtra">PMID:010706635</ref><ref group="xtra">PMID:011587640</ref><references group="xtra"/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Amzel, L M.]]
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[[Category: Large Structures]]
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[[Category: Bianchet, M A.]]
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[[Category: Amzel LM]]
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[[Category: Chen, S.]]
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[[Category: Bianchet MA]]
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[[Category: Faig, M.]]
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[[Category: Chen S]]
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[[Category: Ross, D.]]
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[[Category: Faig M]]
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[[Category: Winski, S.]]
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[[Category: Ross D]]
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[[Category: Flavoprotein]]
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[[Category: Winski S]]
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[[Category: Oxidoreductase]]
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[[Category: Rossman fold]]
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Current revision

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION

PDB ID 1d4a

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