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3nhu

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nhu RCSB], [http://www.ebi.ac.uk/pdbsum/3nhu PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nhu RCSB], [http://www.ebi.ac.uk/pdbsum/3nhu PDBsum]</span></td></tr>
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== Function ==
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[[http://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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 14:13, 24 December 2014

X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2

3nhu, resolution 1.90Å

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