5a4k: Difference between revisions

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'''Unreleased structure'''


The entry 5a4k is ON HOLD  until Paper Publication
==Crystal structure of the R139W variant of human NAD(P)H:quinone oxidoreductase==
 
<StructureSection load='5a4k' size='340' side='right' caption='[[5a4k]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
Authors: Lienhart, W.D., Strandback, E., Gudipati, V., Uhl, M.K., Rantase, D.M., Zangger, K., Gruber, K., Macheroux, P.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5a4k]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A4K FirstGlance]. <br>
Description: Crystal structure of the R139W variant of human NAD(P)H:quinone oxidoreductase
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><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>
[[Category: Uhl, M.K]]
<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=5a4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a4k OCA], [http://pdbe.org/5a4k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a4k RCSB], [http://www.ebi.ac.uk/pdbsum/5a4k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a4k ProSAT]</span></td></tr>
[[Category: Strandback, E]]
</table>
[[Category: Zangger, K]]
== Function ==
[[http://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.
__TOC__
</StructureSection>
[[Category: Gruber, K]]
[[Category: Gruber, K]]
[[Category: Gudipati, V]]
[[Category: Gudipati, V]]
[[Category: Lienhart, W.D]]
[[Category: Lienhart, W D]]
[[Category: Macheroux, P]]
[[Category: Macheroux, P]]
[[Category: Rantase, D.M]]
[[Category: Rantase, D M]]
[[Category: Strandback, E]]
[[Category: Uhl, M K]]
[[Category: Zangger, K]]
[[Category: Drug metabolism]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Nqo1]]
[[Category: Oxidative stress]]
[[Category: Oxidoreductase]]
[[Category: Quinone reductase]]
[[Category: Single amino acid exchange]]

Revision as of 10:16, 13 July 2016

Crystal structure of the R139W variant of human NAD(P)H:quinone oxidoreductase

5a4k, resolution 2.09Å

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