4fgj

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{{STRUCTURE_4fgj| PDB=4fgj | SCENE= }}
 
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===Oxidized quinone reductase 2 in complex with primaquine===
 
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==About this Structure==
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==Oxidized quinone reductase 2 in complex with primaquine==
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[[4fgj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGJ OCA].
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<StructureSection load='4fgj' size='340' side='right'caption='[[4fgj]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4fgj]] 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=4FGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.346&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PQ:(4S)-N~4~-(6-METHOXYQUINOLIN-8-YL)PENTANE-1,4-DIAMINE'>1PQ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgj OCA], [https://pdbe.org/4fgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fgj RCSB], [https://www.ebi.ac.uk/pdbsum/4fgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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==See Also==
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*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Leung, K K.]]
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[[Category: Large Structures]]
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[[Category: Shilton, B H.]]
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[[Category: Leung KK]]
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[[Category: Cytosol]]
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[[Category: Shilton BH]]
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[[Category: Fad binding]]
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[[Category: Fmn reductase superfamily]]
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[[Category: Metallo-flavoprotein]]
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[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
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[[Category: Primaquine]]
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[[Category: Rossmann fold]]
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[[Category: Two-electron reduction of quinones to hydroquinone]]
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[[Category: Zn binding]]
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Current revision

Oxidized quinone reductase 2 in complex with primaquine

PDB ID 4fgj

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