4qoe: Difference between revisions
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<StructureSection load='4qoe' size='340' side='right'caption='[[4qoe]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='4qoe' size='340' side='right'caption='[[4qoe]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qoe]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4qoe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qoe OCA], [https://pdbe.org/4qoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qoe RCSB], [https://www.ebi.ac.uk/pdbsum/4qoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qoe ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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> | ||
==See Also== | |||
*[[Quinone reductase|Quinone reductase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Antoine | [[Category: Antoine M]] | ||
[[Category: Boutin | [[Category: Boutin JA]] | ||
[[Category: Ferry | [[Category: Ferry G]] | ||
[[Category: Isabet | [[Category: Isabet T]] | ||
[[Category: Serriere | [[Category: Serriere J]] | ||
Revision as of 13:43, 22 February 2023
The value 'crystal structure of fad quinone reductase 2 at 1.45A
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