3aec: Difference between revisions
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<StructureSection load='3aec' size='340' side='right'caption='[[3aec]], [[Resolution|resolution]] 3.61Å' scene=''> | <StructureSection load='3aec' size='340' side='right'caption='[[3aec]], [[Resolution|resolution]] 3.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3aec]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3aec]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EBM:2-IODO-N-(1-METHYLETHYL)BENZAMIDE'>EBM</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=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=EBM:2-IODO-N-(1-METHYLETHYL)BENZAMIDE'>EBM</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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae5|3ae5]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3ae9|3ae9]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aed|3aed]], [[3aee|3aee]], [[3aef|3aef]], [[3aeg|3aeg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae5|3ae5]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3ae9|3ae9]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aed|3aed]], [[3aee|3aee]], [[3aef|3aef]], [[3aeg|3aeg]]</div></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/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aec OCA], [https://pdbe.org/3aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aec RCSB], [https://www.ebi.ac.uk/pdbsum/3aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aec ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/DHSD_PIG DHSD_PIG]] 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). [[https://www.uniprot.org/uniprot/SDHA_PIG SDHA_PIG]] 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). Can act as a tumor suppressor (By similarity). [[https://www.uniprot.org/uniprot/C560_PIG C560_PIG]] 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).<ref>PMID:17480203</ref> [[https://www.uniprot.org/uniprot/SDHB_PIG SDHB_PIG]] Iron-sulfur protein (IP) 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). | ||
==See Also== | ==See Also== | ||
*[[Succinate | *[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:24, 22 December 2021
Crystal structure of porcine heart mitochondrial complex II bound with 2-Iodo-N-(1-methylethyl)-benzamid
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Large Structures
- Pig
- Harada, S
- Honma, T
- Inaoka, D K
- Inoue, M
- Kido, Y
- Kita, K
- Mao, J
- Matsuoka, S
- Omori, J
- Osanai, A
- Sakamoto, K
- Sasaki, T
- Shindo, M
- Tanaka, A
- Electron transport
- Fad-binding protein
- Heme
- Inhibitor
- Iron
- Iron-sulfur
- Metal-binding
- Mitochondrion
- Mitochondrion inner membrane
- Oxidoreductase
- Oxidoreductase-oxidoreductase inhibitor complex
- Respiratory complex ii
- Transit peptide
- Transmembrane
- Transport
- Tricarboxylic acid cycle
