4fgl: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fgl]] is a 4 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=4FGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGL FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fgl]] is a 4 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=4FGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLQ:N4-(7-CHLORO-QUINOLIN-4-YL)-N1,N1-DIETHYL-PENTANE-1,4-DIAMINE'>CLQ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLQ:N4-(7-CHLORO-QUINOLIN-4-YL)-N1,N1-DIETHYL-PENTANE-1,4-DIAMINE'>CLQ</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=4fgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgl OCA], [https://pdbe.org/4fgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fgl RCSB], [https://www.ebi.ac.uk/pdbsum/4fgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgl ProSAT]</span></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=4fgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgl OCA], [https://pdbe.org/4fgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fgl RCSB], [https://www.ebi.ac.uk/pdbsum/4fgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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==See Also== | ==See Also== | ||
*[[Quinone reductase|Quinone reductase]] | *[[Quinone reductase 3D structures|Quinone reductase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 18:24, 14 March 2024
Reduced quinone reductase 2 in complex with chloroquineReduced quinone reductase 2 in complex with chloroquine
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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