5j4z
From Proteopedia
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<SX load='5j4z' size='340' side='right' viewer='molstar' caption='[[5j4z]], [[Resolution|resolution]] 5.80Å' scene=''> | <SX load='5j4z' size='340' side='right' viewer='molstar' caption='[[5j4z]], [[Resolution|resolution]] 5.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5j4z]] is a | + | <table><tr><td colspan='2'>[[5j4z]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J4Z FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.8Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=5j4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4z OCA], [https://pdbe.org/5j4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j4z RCSB], [https://www.ebi.ac.uk/pdbsum/5j4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j4z ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
- | == Function == | ||
- | [[http://www.uniprot.org/uniprot/COX2_SHEEP COX2_SHEEP]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. [[http://www.uniprot.org/uniprot/W5P2X9_SHEEP W5P2X9_SHEEP]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.[RuleBase:RU004494] [[http://www.uniprot.org/uniprot/COX3_SHEEP COX3_SHEEP]] Subunits I, II and III form the functional core of the enzyme complex. [[http://www.uniprot.org/uniprot/B9VH04_SHEEP B9VH04_SHEEP]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.[PIRNR:PIRNR000019] [[http://www.uniprot.org/uniprot/COX1_SHEEP COX1_SHEEP]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. [[http://www.uniprot.org/uniprot/CYB_SHEEP CYB_SHEEP]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
- | + | [[Category: Fiedorczuk K]] | |
- | [[Category: Fiedorczuk | + | [[Category: Letts JA]] |
- | [[Category: Letts | + | [[Category: Sazanov LA]] |
- | [[Category: Sazanov | + | |
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Current revision
Architecture of tight respirasome
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