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==Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with dicoumarol at 2.2 A resolution==
==Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with dicoumarol at 2.2 A resolution==
<StructureSection load='4cet' size='340' side='right' caption='[[4cet]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='4cet' size='340' side='right'caption='[[4cet]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cet]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CET FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cet]] is a 1 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=4CET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CET FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTC:BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-BENZOPYRONE]'>DTC</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTC:BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-BENZOPYRONE]'>DTC</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cet OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cet RCSB], [http://www.ebi.ac.uk/pdbsum/4cet PDBsum]</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=4cet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cet OCA], [https://pdbe.org/4cet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cet RCSB], [https://www.ebi.ac.uk/pdbsum/4cet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cet ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4cet" style="background-color:#fffaf0;"></div>
==See Also==
*[[NADPH dehydrogenase|NADPH dehydrogenase]]
*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Binter, A.]]
[[Category: Homo sapiens]]
[[Category: Gruber, K.]]
[[Category: Large Structures]]
[[Category: Gudipati, V.]]
[[Category: Binter A]]
[[Category: Lienhart, W D.]]
[[Category: Gruber K]]
[[Category: Macheroux, P.]]
[[Category: Gudipati V]]
[[Category: Pulido, S.]]
[[Category: Lienhart WD]]
[[Category: Saf, R.]]
[[Category: Macheroux P]]
[[Category: Uhl, M K.]]
[[Category: Pulido S]]
[[Category: Zangger, K.]]
[[Category: Saf R]]
[[Category: Coumarin-based inhibitor]]
[[Category: Uhl MK]]
[[Category: Fad]]
[[Category: Zangger K]]
[[Category: Flavoprotein]]
[[Category: Nad]]
[[Category: Nadp]]
[[Category: Nadph]]
[[Category: Nq01]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-inhibitor complex]]
[[Category: P187]]
[[Category: Single amino acid exchange]]

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