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4xdg
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal Structure of Quinone Reductase II in complex with 2-(4-aminophenyl)-5-methoxy-1-oxy-indol-3-one molecule== |
| - | + | <StructureSection load='4xdg' size='340' side='right' caption='[[4xdg]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4xdg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XDG FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3ZU:(2S)-2-(4-AMINOPHENYL)-1-HYDROXY-5-METHOXY-1,2-DIHYDRO-3H-INDOL-3-ONE'>3ZU</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4xdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xdg OCA], [http://pdbe.org/4xdg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xdg RCSB], [http://www.ebi.ac.uk/pdbsum/4xdg PDBsum]</span></td></tr> | |
| - | [[Category: | + | </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: Boutin, J A]] | ||
[[Category: Ferry, G]] | [[Category: Ferry, G]] | ||
| - | [[Category: | + | [[Category: Isabet, T]] |
[[Category: Nepveu, F]] | [[Category: Nepveu, F]] | ||
[[Category: Sirigu, S]] | [[Category: Sirigu, S]] | ||
| - | [[Category: | + | [[Category: Thompson, A]] |
[[Category: Vuillard, L]] | [[Category: Vuillard, L]] | ||
| - | [[Category: | + | [[Category: Fad]] |
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Indolone oxide]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Qr2]] | ||
Revision as of 20:22, 13 January 2016
Crystal Structure of Quinone Reductase II in complex with 2-(4-aminophenyl)-5-methoxy-1-oxy-indol-3-one molecule
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Categories: Boutin, J A | Ferry, G | Isabet, T | Nepveu, F | Sirigu, S | Thompson, A | Vuillard, L | Fad | Flavoprotein | Indolone oxide | Metal-binding | Oxidoreductase | Qr2
