3ox2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values== | |
| + | <StructureSection load='3ox2' size='340' side='right'caption='[[3ox2]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ox2]] 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=3OX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OX2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=79X:2-HYDROXY-8,9-DIMETHOXY-6H-ISOINDOLO[2,1-A]INDOL-6-ONE'>79X</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=3ox2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox2 OCA], [https://pdbe.org/3ox2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ox2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ox2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 3D structures|Quinone reductase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mesecar AD]] | ||
| + | [[Category: Pegan SD]] | ||
| + | [[Category: Sturdy M]] | ||
Current revision
X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values
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