5fuq: Difference between revisions
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<StructureSection load='5fuq' size='340' side='right'caption='[[5fuq]], [[Resolution|resolution]] 2.04Å' scene=''> | <StructureSection load='5fuq' size='340' side='right'caption='[[5fuq]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fuq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5fuq]] 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=5FUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FUQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DTC:BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-BENZOPYRONE]'>DTC</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DTC:BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-BENZOPYRONE]'>DTC</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fuq OCA], [https://pdbe.org/5fuq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fuq RCSB], [https://www.ebi.ac.uk/pdbsum/5fuq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fuq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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. | ||
==See Also== | ==See Also== | ||
*[[NADPH dehydrogenase|NADPH dehydrogenase]] | *[[NADPH dehydrogenase|NADPH dehydrogenase]] | ||
*[[Quinone reductase|Quinone reductase]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gavira | [[Category: Gavira JA]] | ||
[[Category: Medina-Carmona | [[Category: Medina-Carmona E]] | ||
[[Category: Pey | [[Category: Pey AL]] | ||
Revision as of 13:27, 26 July 2023
CRYSTAL STRUCTURE OF THE H80R VARIANT OF NQO1 BOUND TO DICOUMAROL
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