3owh
From Proteopedia
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| - | [[Image:3owh.png|left|200px]] | ||
| - | + | ==X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values== | |
| - | + | <StructureSection load='3owh' size='340' side='right'caption='[[3owh]], [[Resolution|resolution]] 2.28Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3owh]] 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=3OWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OWH 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]] 2.28Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=52X:METHYL+{3-[2-(ACETYLAMINO)ETHYL]-2-IODO-1H-INDOL-5-YL}CARBAMATE'>52X</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=3owh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3owh OCA], [https://pdbe.org/3owh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3owh RCSB], [https://www.ebi.ac.uk/pdbsum/3owh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3owh ProSAT]</span></td></tr> |
| - | [[3owh]] is a 2 chain structure with sequence from [ | + | </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== | ==See Also== | ||
| - | *[[Quinone reductase|Quinone reductase]] | + | *[[Quinone reductase 3D structures|Quinone reductase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mesecar AD]] |
| - | [[Category: | + | [[Category: Pegan SD]] |
| - | [[Category: | + | [[Category: Sturdy M]] |
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Current revision
X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values
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