4ysz: Difference between revisions

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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 ==
<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>
<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>
</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>
</td></tr><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=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>
<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>
<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>
<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'>[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>
</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/Q33862_ASCSU Q33862_ASCSU]  
<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==
*[[Succinate Dehydrogenase|Succinate Dehydrogenase]]
*[[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]]
[[Category: Harada, S]]
[[Category: Harada S]]
[[Category: Honma, T]]
[[Category: Honma T]]
[[Category: Inaoka, D K]]
[[Category: Inaoka DK]]
[[Category: Inoue, M]]
[[Category: Inoue M]]
[[Category: Kita, K]]
[[Category: Kita K]]
[[Category: Nagahama, M]]
[[Category: Nagahama M]]
[[Category: Sakamoto, K]]
[[Category: Sakamoto K]]
[[Category: Sato, D]]
[[Category: Sato D]]
[[Category: Shiba, T]]
[[Category: Shiba T]]
[[Category: Yamamoto, A]]
[[Category: Yamamoto A]]
[[Category: Yone, A]]
[[Category: Yone A]]
[[Category: Complex ii]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Rhodoquinol-fumarate reductase]]
Retrieved from "https://proteopedia.org/4ysz"