2b0m: Difference between revisions

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New page: left|200px<br /> <applet load="2b0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b0m, resolution 2.00Å" /> '''Human dihydroorotat...
 
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[[Image:2b0m.gif|left|200px]]<br />
<applet load="2b0m" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2b0m, resolution 2.00&Aring;" />
'''Human dihydroorotate dehydrogenase bound to a novel inhibitor'''<br />


==About this Structure==
==Human dihydroorotate dehydrogenase bound to a novel inhibitor==
2B0M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with 201, FMN and ORO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydroorotate_oxidase Dihydroorotate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.1 1.3.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B0M OCA].  
<StructureSection load='2b0m' size='340' side='right'caption='[[2b0m]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
[[Category: Dihydroorotate oxidase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[2b0m]] is a 1 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=2B0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B0M FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=201:3-AMIDO-5-BIPHENYL-BENZOIC+ACID'>201</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene></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=2b0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0m OCA], [https://pdbe.org/2b0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b0m RCSB], [https://www.ebi.ac.uk/pdbsum/2b0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b0m ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/PYRD_HUMAN PYRD_HUMAN] Defects in DHODH are the cause of postaxial acrofacial dysostosis (POADS) [MIM:[https://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 ==
[https://www.uniprot.org/uniprot/PYRD_HUMAN PYRD_HUMAN] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/2b0m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b0m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Therapeutic agents brequinar sodium and leflunomide (Arava) work by binding in a hydrophobic tunnel formed by a highly variable N-terminus of family 2 dihydroorotate dehydrogenase (DHODH). The X-ray crystallographic structure of an analog of brequinar bound to human DHODH was determined. In silico screening of a library of compounds suggested another subset of brequinar analogs that do not inhibit human DHODH as potentially effective inhibitors of Plasmodium falciparum DHODH.
 
Brequinar derivatives and species-specific drug design for dihydroorotate dehydrogenase.,Hurt DE, Sutton AE, Clardy J Bioorg Med Chem Lett. 2006 Mar 15;16(6):1610-5. Epub 2006 Jan 10. PMID:16406782<ref>PMID:16406782</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2b0m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Dihydroorotate dehydrogenase|Dihydroorotate dehydrogenase]]
*[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Clardy, J.]]
[[Category: Clardy J]]
[[Category: Hurt, D.E.]]
[[Category: Hurt DE]]
[[Category: Sutton, A.E.]]
[[Category: Sutton AE]]
[[Category: 201]]
[[Category: FMN]]
[[Category: ORO]]
[[Category: tim barrel; alpha/beta barrel]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:56:51 2007''

Latest revision as of 07:32, 23 August 2023

Human dihydroorotate dehydrogenase bound to a novel inhibitor

2b0m, resolution 2.00Å

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