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5dfs

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<StructureSection load='5dfs' size='340' side='right'caption='[[5dfs]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='5dfs' size='340' side='right'caption='[[5dfs]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dfs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atesp Atesp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dfs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ateles_sp. Ateles sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYCS, CYC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9511 ATESP])</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=5dfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfs OCA], [https://pdbe.org/5dfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dfs RCSB], [https://www.ebi.ac.uk/pdbsum/5dfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfs ProSAT]</span></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=5dfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfs OCA], [https://pdbe.org/5dfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dfs RCSB], [https://www.ebi.ac.uk/pdbsum/5dfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CYC_ATESP CYC_ATESP]] 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).
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[https://www.uniprot.org/uniprot/CYC_ATESP CYC_ATESP] 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 ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atesp]]
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[[Category: Ateles sp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: BOWLER, B E]]
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[[Category: BOWLER BE]]
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[[Category: Goldes, M E]]
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[[Category: Goldes ME]]
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[[Category: Jeakins-Cooley, M E]]
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[[Category: Jeakins-Cooley ME]]
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[[Category: MOU, T C]]
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[[Category: MOU TC]]
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[[Category: McClelland, L J]]
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[[Category: McClelland LJ]]
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[[Category: SPRANG, S R]]
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[[Category: SPRANG SR]]
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[[Category: Electron transport]]
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[[Category: Mitochondrial cytochrome c]]
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Revision as of 10:33, 21 June 2023

Crystal structure of Spider Monkey Cytochrome C at 1.15 Angstrom

PDB ID 5dfs

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