5c0z: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='5c0z' size='340' side='right'caption='[[5c0z]], [[Resolution|resolution]] 1.12Å' scene=''> | <StructureSection load='5c0z' size='340' side='right'caption='[[5c0z]], [[Resolution|resolution]] 1.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c0z]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5c0z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C0Z FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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=5c0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0z OCA], [https://pdbe.org/5c0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c0z RCSB], [https://www.ebi.ac.uk/pdbsum/5c0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c0z ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CYC_RAT CYC_RAT] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 26: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Brunzelle | [[Category: Rattus norvegicus]] | ||
[[Category: Edwards | [[Category: Brunzelle JS]] | ||
[[Category: Huttemann | [[Category: Edwards BFP]] | ||
[[Category: Mahapatra | [[Category: Huttemann M]] | ||
[[Category: Vaishnav | [[Category: Mahapatra G]] | ||
[[Category: Vaishnav AA]] | |||