4rr4: Difference between revisions

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New page: '''Unreleased structure''' The entry 4rr4 is ON HOLD until Paper Publication Authors: Zhu, L., Ren, X., Zhu, J., Li, H. Description: Crystal structure of human dihydroorotate dehydroge...
 
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'''Unreleased structure'''


The entry 4rr4 is ON HOLD  until Paper Publication
==Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A367==
<StructureSection load='4rr4' size='340' side='right'caption='[[4rr4]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rr4]] 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=4RR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RR4 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]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3V1:2-CHLORO-N-[3-(4-{[(2Z)-2-CYANO-3-CYCLOPROPYL-3-HYDROXYPROP-2-ENOYL]AMINO}PHENOXY)PHENYL]-4-METHYL-1,3-THIAZOLE-5-CARBOXAMIDE'>3V1</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr4 OCA], [https://pdbe.org/4rr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rr4 RCSB], [https://www.ebi.ac.uk/pdbsum/4rr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr4 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.


Authors: Zhu, L., Ren, X., Zhu, J., Li, H.
==See Also==
 
*[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]]
Description: Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A367
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Li H]]
[[Category: Ren X]]
[[Category: Zhu J]]
[[Category: Zhu L]]

Latest revision as of 20:54, 20 September 2023

Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A367Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A367

Structural highlights

4rr4 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.38Å
Ligands:, , ,
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.

See Also

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

4rr4, resolution 2.38Å

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OCA