4jgd: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A016==
 
<StructureSection load='4jgd' size='340' side='right' caption='[[4jgd]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
The entry 4jgd is ON HOLD until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4jgd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JGD FirstGlance]. <br>
Authors: Zhu, L., Zhu, J., Ren, X.
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4JG:1-[4-METHYL-2-(NAPHTHALEN-2-YLAMINO)-1,3-THIAZOL-5-YL]ETHANONE'>4JG</scene>, <scene name='pdbligand=DET:UNDECYLAMINE-N,N-DIMETHYL-N-OXIDE'>DET</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><br>
 
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHODH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
Description: Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A016
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jgd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jgd RCSB], [http://www.ebi.ac.uk/pdbsum/4jgd PDBsum]</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: Human]]
[[Category: Li, H.]]
[[Category: Ren, X.]]
[[Category: Zhu, J.]]
[[Category: Zhu, L.]]
[[Category: Dihydroorotate dehydrogenase]]
[[Category: Inhibitor]]
[[Category: Oxidoreductase]]

Revision as of 15:08, 18 May 2014

Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A016Crystal structure of human dihydroorotate dehydrogenase (DHODH) with DH03A016

Structural highlights

4jgd is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Gene:DHODH (HUMAN)
Activity:Dihydroorotate dehydrogenase (quinone), with EC number 1.3.5.2
Resources:FirstGlance, OCA, RCSB, PDBsum

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

4jgd, resolution 2.05Å

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