5a4k
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the R139W variant of human NAD(P)H:quinone oxidoreductase== | |
| - | + | <StructureSection load='5a4k' size='340' side='right' caption='[[5a4k]], [[Resolution|resolution]] 2.09Å' scene=''> | |
| - | + | == 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> | |
| - | + | </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> | |
| - | [ | + | <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> |
| - | [[ | + | <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> |
| - | [ | + | </table> |
| - | [[ | + | == 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 | + | [[Category: Lienhart, W D]] |
[[Category: Macheroux, P]] | [[Category: Macheroux, P]] | ||
| - | [[Category: Rantase, D | + | [[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
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