5hqe
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human dihydroorotate dehydrogenase (DHODH) with compound 18T== | |
| - | + | <StructureSection load='5hqe' size='340' side='right' caption='[[5hqe]], [[Resolution|resolution]] 1.62Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5hqe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HQE FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=64B:METHYL+(2Z)-CYANO[3-(2-FLUORO-4-METHOXYPHENYL)-4-OXO-1,3-THIAZOLIDIN-2-YLIDENE]ACETATE'>64B</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotate_dehydrogenase_(quinone) Dihydroorotate dehydrogenase (quinone)], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqe OCA], [http://pdbe.org/5hqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hqe RCSB], [http://www.ebi.ac.uk/pdbsum/5hqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/PYRD_HUMAN PYRD_HUMAN]] Defects in DHODH are the cause of postaxial acrofacial dysostosis (POADS) [MIM:[http://omim.org/entry/263750 263750]]; also known as Miller syndrome. POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases.<ref>PMID:19915526</ref> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PYRD_HUMAN PYRD_HUMAN]] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Huang, J]] | ||
| + | [[Category: Lu, Q]] | ||
| + | [[Category: Wu, D]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Oxidoreductase-inhibitor complex]] | ||
Revision as of 15:43, 27 July 2016
Crystal structure of human dihydroorotate dehydrogenase (DHODH) with compound 18T
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