5df5: Difference between revisions

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-'''Unreleased structure'''
-The entry 5df5 is ON HOLD  until Paper Publication
+==The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.==
+<StructureSection load='5df5' size='340' side='right'caption='[[5df5]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5df5]] 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=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.301&#8491;</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [https://pdbe.org/5df5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [https://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr>
+</table>
+== 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).
-Authors: Edwards, B.F.P., Mahapatra, G., Vaishnav, A.A., Brunzelle, J.S., Huttemann, M.
+==See Also==
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
-Description:
+__TOC__
-[[Category: Unreleased Structures]]
+</StructureSection>
-[[Category: Edwards, B.F.P]]
+[[Category: Large Structures]]
-[[Category: Brunzelle, J.S]]
+[[Category: Rattus norvegicus]]
-[[Category: Vaishnav, A.A]]
+[[Category: Brunzelle JS]]
-[[Category: Mahapatra, G]]
+[[Category: Edwards BFP]]
-[[Category: Huttemann, M]]
+[[Category: Huttemann M]]
+[[Category: Mahapatra G]]
+[[Category: Vaishnav AA]]