3ox2: Difference between revisions
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New page: '''Unreleased structure''' The entry 3ox2 is ON HOLD Authors: Pegan, S.D., Sturdy, M., Mesecar, A.D. Description: X-ray Structural study of quinone reductase II inhibition by compounds... |
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==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]] | |||
Latest revision as of 13:37, 21 February 2024
X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 valuesX-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values
Structural highlights
FunctionNQO2_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.[1] See AlsoReferences
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