2lit: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lit RCSB], [http://www.ebi.ac.uk/pdbsum/2lit PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lit RCSB], [http://www.ebi.ac.uk/pdbsum/2lit PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST]] 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
