3ovm
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3ovm.png|left|200px]] | ||
| - | + | ==X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values== | |
| - | + | <StructureSection load='3ovm' size='340' side='right'caption='[[3ovm]], [[Resolution|resolution]] 2.09Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ovm]] 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=3OVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OVM 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]] 2.09Å</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=MZC:METHYL+{3-[2-(ACETYLAMINO)ETHYL]-1H-INDOL-5-YL}CARBAMATE'>MZC</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=3ovm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ovm OCA], [https://pdbe.org/3ovm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ovm RCSB], [https://www.ebi.ac.uk/pdbsum/3ovm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ovm ProSAT]</span></td></tr> |
| - | [[3ovm]] 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: Boutin | + | [[Category: Large Structures]] |
| - | [[Category: Delagrange | + | [[Category: Boutin JA]] |
| - | [[Category: Ferry | + | [[Category: Delagrange P]] |
| - | [[Category: Pegan | + | [[Category: Ferry G]] |
| - | [[Category: Sturdy | + | [[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
| |||||||||||
