7t6h
From Proteopedia
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==E. coli dihydroorotate dehydrogenase== | ==E. coli dihydroorotate dehydrogenase== | ||
| - | <StructureSection load='7t6h' size='340' side='right'caption='[[7t6h]]' scene=''> | + | <StructureSection load='7t6h' size='340' side='right'caption='[[7t6h]], [[Resolution|resolution]] 2.42Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T6H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7t6h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T6H FirstGlance]. <br> |
| - | </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=7t6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t6h OCA], [https://pdbe.org/7t6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t6h RCSB], [https://www.ebi.ac.uk/pdbsum/7t6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t6h ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7t5k|7t5k]], [[7t5y|7t5y]], [[7t6c|7t6c]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydroorotate_dehydrogenase_(quinone) Dihydroorotate dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.2 1.3.5.2] </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=7t6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t6h OCA], [https://pdbe.org/7t6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t6h RCSB], [https://www.ebi.ac.uk/pdbsum/7t6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t6h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/PYRD_ECOLI PYRD_ECOLI]] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.<ref>PMID:10074342</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hydroxyalkylquinolines (HAQs) are ubiquitious natural products but their interactions with associated protein targets remain elusive. We report X-ray crystal structures of two HAQs in complex with dihydroorotate dehydrogenase (DHODH). Our results reveal the structural basis of DHODH inhibition by HAQs and open the door to downstream structure-activity relationship studies. | ||
| + | |||
| + | Structural insights into inhibition of the drug target dihydroorotate dehydrogenase by bacterial hydroxyalkylquinolines.,Horwitz SM, Blue TC, Ambarian JA, Hoshino S, Seyedsayamdost MR, Davis KM RSC Chem Biol. 2022 Feb 7;3(4):420-425. doi: 10.1039/d1cb00255d. eCollection 2022, Apr 6. PMID:35441142<ref>PMID:35441142</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7t6h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ambarian | + | [[Category: Ambarian, J A]] |
| - | [[Category: Davis | + | [[Category: Davis, K M]] |
| - | [[Category: Horwitz | + | [[Category: Horwitz, S M]] |
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]] | ||
Revision as of 07:34, 29 June 2022
E. coli dihydroorotate dehydrogenase
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