6oc1: Difference between revisions

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'''Unreleased structure'''


The entry 6oc1 is ON HOLD  until Paper Publication
==Crystal structure of human DHODH with TAK-632==
 
<StructureSection load='6oc1' size='340' side='right'caption='[[6oc1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
Authors: Durst, M.A., Lavie, A.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6oc1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OC1 FirstGlance]. <br>
Description: Crystal structure of human DHODH with TAK-632
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1SU:N-{7-CYANO-6-[4-FLUORO-3-({[3-(TRIFLUOROMETHYL)PHENYL]ACETYL}AMINO)PHENOXY]-1,3-BENZOTHIAZOL-2-YL}CYCLOPROPANECARBOXAMIDE'>1SU</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
[[Category: Unreleased Structures]]
<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>
[[Category: Durst, M.A]]
<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=6oc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oc1 OCA], [http://pdbe.org/6oc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oc1 RCSB], [http://www.ebi.ac.uk/pdbsum/6oc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oc1 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: Large Structures]]
[[Category: Durst, M A]]
[[Category: Lavie, A]]
[[Category: Lavie, A]]
[[Category: Dhodh]]
[[Category: Inhibitor]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Tak-632]]

Revision as of 14:06, 13 November 2019

Crystal structure of human DHODH with TAK-632Crystal structure of human DHODH with TAK-632

Structural highlights

6oc1 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Activity:Dihydroorotate dehydrogenase (quinone), with EC number 1.3.5.2
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[PYRD_HUMAN] Defects in DHODH are the cause of postaxial acrofacial dysostosis (POADS) [MIM: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.[1]

Function

[PYRD_HUMAN] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

References

  1. ↑ Ng SB, Buckingham KJ, Lee C, Bigham AW, Tabor HK, Dent KM, Huff CD, Shannon PT, Jabs EW, Nickerson DA, Shendure J, Bamshad MJ. Exome sequencing identifies the cause of a mendelian disorder. Nat Genet. 2010 Jan;42(1):30-5. doi: 10.1038/ng.499. Epub 2009 Nov 13. PMID:19915526 doi:10.1038/ng.499

6oc1, resolution 2.70Å

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