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==Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with N-biphenyl-3-yl-2-(trifluoromethyl)benzamide==
==Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with N-biphenyl-3-yl-2-(trifluoromethyl)benzamide==
<StructureSection load='4ytm' size='340' side='right' caption='[[4ytm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='4ytm' size='340' side='right'caption='[[4ytm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ytm]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YTM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ytm]] 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=4YTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YTM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=F6A:N-BIPHENYL-3-YL-2-(TRIFLUOROMETHYL)BENZAMIDE'>F6A</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ysx|4ysx]], [[4ysy|4ysy]], [[4ysz|4ysz]], [[4yt0|4yt0]], [[4ytn|4ytn]], [[4ytp|4ytp]], [[4yxd|4yxd]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=F6A:N-BIPHENYL-3-YL-2-(TRIFLUOROMETHYL)BENZAMIDE'>F6A</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </span></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=4ytm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ytm OCA], [https://pdbe.org/4ytm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ytm RCSB], [https://www.ebi.ac.uk/pdbsum/4ytm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ytm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ytm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ytm OCA], [http://pdbe.org/4ytm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ytm RCSB], [http://www.ebi.ac.uk/pdbsum/4ytm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ytm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DHSD_ASCSU DHSD_ASCSU]] Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity). [[http://www.uniprot.org/uniprot/U1LRQ3_ASCSU U1LRQ3_ASCSU]] Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).[RuleBase:RU362051]
[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4ytm" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4ytm" style="background-color:#fffaf0;"></div>
==See Also==
*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Harada, S]]
[[Category: Large Structures]]
[[Category: Honma, T]]
[[Category: Harada S]]
[[Category: Inaoka, D K]]
[[Category: Honma T]]
[[Category: Inoue, M]]
[[Category: Inaoka DK]]
[[Category: Kita, K]]
[[Category: Inoue M]]
[[Category: Nagahama, M]]
[[Category: Kita K]]
[[Category: Sakamoto, K]]
[[Category: Nagahama M]]
[[Category: Sato, D]]
[[Category: Sakamoto K]]
[[Category: Shiba, T]]
[[Category: Sato D]]
[[Category: Yamamoto, A]]
[[Category: Shiba T]]
[[Category: Yone, A]]
[[Category: Yamamoto A]]
[[Category: Complex ii]]
[[Category: Yone A]]
[[Category: Inhibitor]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Rhodoquinol-fumarate reductase]]
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