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4qoe
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==The value 'crystal structure of fad quinone reductase 2 at 1.45A== |
| - | + | <StructureSection load='4qoe' size='340' side='right' caption='[[4qoe]], [[Resolution|resolution]] 1.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4qoe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QOE FirstGlance]. <br> | |
| - | + | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qod|4qod]], [[4qof|4qof]], [[4qog|4qog]], [[4qoh|4qoh]], [[4qoi|4qoi]], [[4qoj|4qoj]]</td></tr> | |
| - | + | <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> | |
| - | [[ | + | <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=4qoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qoe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qoe RCSB], [http://www.ebi.ac.uk/pdbsum/4qoe PDBsum]</span></td></tr> |
| - | [[ | + | </table> |
| + | == Function == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Antoine, M]] | [[Category: Antoine, M]] | ||
| - | [[Category: | + | [[Category: Boutin, J A]] |
| + | [[Category: Ferry, G]] | ||
[[Category: Isabet, T]] | [[Category: Isabet, T]] | ||
| - | [[Category: | + | [[Category: Serriere, J]] |
| + | [[Category: Flavin adenine dinucleotide]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Oxidoreductase flavoprotein]] | ||
Revision as of 12:18, 1 July 2015
The value 'crystal structure of fad quinone reductase 2 at 1.45A
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