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3f1q
From Proteopedia
(Difference between revisions)
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==Human dihydroorotate dehydrogenase in complex with a leflunomide derivative inhibitor 1== | ==Human dihydroorotate dehydrogenase in complex with a leflunomide derivative inhibitor 1== | ||
| - | <StructureSection load='3f1q' size='340' side='right' caption='[[3f1q]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3f1q' size='340' side='right'caption='[[3f1q]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3f1q]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3f1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F1Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BCE:(2Z)-N-BIPHENYL-4-YL-2-CYANO-3-HYDROXYBUT-2-ENAMIDE'>BCE</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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BCE:(2Z)-N-BIPHENYL-4-YL-2-CYANO-3-HYDROXYBUT-2-ENAMIDE'>BCE</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHODH ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHODH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydroorotate_oxidase_(fumarate) Dihydroorotate oxidase (fumarate)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.98.1 1.3.98.1] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3f1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f1q OCA], [https://pdbe.org/3f1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f1q RCSB], [https://www.ebi.ac.uk/pdbsum/3f1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f1q ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == 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 == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PYRD_HUMAN PYRD_HUMAN]] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Dihydroorotate dehydrogenase|Dihydroorotate dehydrogenase]] | + | *[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Davies, M]] | [[Category: Davies, M]] | ||
[[Category: Fishwick, C W.G]] | [[Category: Fishwick, C W.G]] | ||
Revision as of 09:21, 23 February 2022
Human dihydroorotate dehydrogenase in complex with a leflunomide derivative inhibitor 1
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Categories: Human | Large Structures | Davies, M | Fishwick, C W.G | Heikkila, T | Johnson, A P | McConkey, G A | Parsons, M R | Dihydroorotate dehydrogenase | Fad | Flavoprotein | Leflunomide | Membrane | Mitochondrion | Mitochondrion inner membrane | Oxidoreductase | Pyrimidine biosynthesis | Transit peptide
