4ysz

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<StructureSection load='4ysz' size='340' side='right'caption='[[4ysz]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='4ysz' size='340' side='right'caption='[[4ysz]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ysz]] 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=4YSZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YSZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ysz]] 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=4YSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YSZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12J:2-IODO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE'>12J</scene>, <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=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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ysx|4ysx]], [[4ysy|4ysy]], [[4yt0|4yt0]], [[4ytm|4ytm]], [[4ytn|4ytn]], [[4ytp|4ytp]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12J:2-IODO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE'>12J</scene>, <scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ysz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ysz OCA], [https://pdbe.org/4ysz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ysz RCSB], [https://www.ebi.ac.uk/pdbsum/4ysz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ysz ProSAT]</span></td></tr>
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<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=4ysz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ysz OCA], [http://pdbe.org/4ysz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ysz RCSB], [http://www.ebi.ac.uk/pdbsum/4ysz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ysz ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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]
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[https://www.uniprot.org/uniprot/SDHB_ASCSU SDHB_ASCSU] Iron-sulfur protein (Ip) subunit of the mitochondrial electron transport chain complex II which, together with the flavoprotein (Fp) subunit forms the catalytic core of the complex (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). During the free-living egg-larvae stages, which occur in an aerobic environment, complex II acts as a succinate dehydrogenase by transferring electrons from succinate to ubiquinone (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, complex II acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436).<ref>PMID:10743611</ref> <ref>PMID:12742584</ref> <ref>PMID:17933581</ref> <ref>PMID:2843227</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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==See Also==
==See Also==
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*[[Succinate Dehydrogenase|Succinate Dehydrogenase]]
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*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Harada, S]]
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[[Category: Harada S]]
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[[Category: Honma, T]]
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[[Category: Honma T]]
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[[Category: Inaoka, D K]]
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[[Category: Inaoka DK]]
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[[Category: Inoue, M]]
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[[Category: Inoue M]]
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[[Category: Kita, K]]
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[[Category: Kita K]]
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[[Category: Nagahama, M]]
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[[Category: Nagahama M]]
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[[Category: Sakamoto, K]]
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[[Category: Sakamoto K]]
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[[Category: Sato, D]]
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[[Category: Sato D]]
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[[Category: Shiba, T]]
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[[Category: Shiba T]]
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[[Category: Yamamoto, A]]
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[[Category: Yamamoto A]]
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[[Category: Yone, A]]
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[[Category: Yone A]]
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[[Category: Complex ii]]
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[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
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[[Category: Rhodoquinol-fumarate reductase]]
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Current revision

Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with 2-iodo-N-[3-(1-methylethoxy)phenyl]benzamide

PDB ID 4ysz

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