4qog: Difference between revisions
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''' | ==Crystal structure of fad quinone reductase 2 in complex with melatonin at 1.4A== | ||
<StructureSection load='4qog' size='340' side='right' caption='[[4qog]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qog]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QOG 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=ML1:N-[2-(5-METHOXY-1H-INDOL-3-YL)ETHYL]ACETAMIDE'>ML1</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]], [[4qoe|4qoe]], [[4qof|4qof]], [[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> | |||
[[Category: | <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=4qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qog RCSB], [http://www.ebi.ac.uk/pdbsum/4qog 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: Boutin, J A]] | |||
[[Category: Ferry, G]] | [[Category: Ferry, G]] | ||
[[Category: | [[Category: Isabet, T]] | ||
[[Category: Serriere, J]] | [[Category: Serriere, J]] | ||
[[Category: | [[Category: Fad melatonin]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: Oxidoreductase flavoprotein]] | |||
Revision as of 12:18, 1 July 2015
Crystal structure of fad quinone reductase 2 in complex with melatonin at 1.4A
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