View source for 4ytn


==Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with N-[3-(pentafluorophenoxy)phenyl]-2-(trifluoromethyl)benzamide==
<StructureSection load='4ytn' size='340' side='right'caption='[[4ytn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ytn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YTN 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FD8:N-[3-(PENTAFLUOROPHENOXY)PHENYL]-2-(TRIFLUOROMETHYL)BENZAMIDE'>FD8</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=4ytn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ytn OCA], [https://pdbe.org/4ytn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ytn RCSB], [https://www.ebi.ac.uk/pdbsum/4ytn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ytn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SDHA1_ASCSU SDHA1_ASCSU] Flavoprotein (Fp) subunit of the mitochondrial electron transport chain complex II which, together with the iron-sulfur protein (Ip) subunit forms the catalytic core of the complex (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436).<ref>PMID:12742584</ref> <ref>PMID:17933581</ref> <ref>PMID:2843227</ref> <ref>PMID:7739664</ref> <ref>PMID:7822332</ref> <ref>PMID:8435436</ref> 

==See Also==
*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ascaris suum]]
[[Category: Large Structures]]
[[Category: Harada S]]
[[Category: Honma T]]
[[Category: Inaoka DK]]
[[Category: Inoue M]]
[[Category: Kita K]]
[[Category: Nagahama M]]
[[Category: Sakamoto K]]
[[Category: Sato D]]
[[Category: Shiba T]]
[[Category: Yamamoto A]]
[[Category: Yone A]]