5ea2: Difference between revisions
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==Crystal Structure of Holo NAD(P)H dehydrogenase, quinone 1== | ==Crystal Structure of Holo NAD(P)H dehydrogenase, quinone 1== | ||
<StructureSection load='5ea2' size='340' side='right' caption='[[5ea2]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='5ea2' size='340' side='right'caption='[[5ea2]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ea2]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ea2]] 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=5EA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EA2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</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></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ea2 OCA], [https://pdbe.org/5ea2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ea2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ea2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ea2 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/NQO1_HUMAN NQO1_HUMAN] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ea2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ea2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Quinone reductase|Quinone reductase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Ahmad | [[Category: Large Structures]] | ||
[[Category: Emadi | [[Category: Ahmad M]] | ||
[[Category: Mbimba | [[Category: Emadi A]] | ||
[[Category: Pidugu | [[Category: Mbimba JE]] | ||
[[Category: Pozharski | [[Category: Pidugu LS]] | ||
[[Category: Sausville | [[Category: Pozharski E]] | ||
[[Category: Toth | [[Category: Sausville EA]] | ||
[[Category: Toth EA]] | |||