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4faa

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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=4faa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4faa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4faa RCSB], [http://www.ebi.ac.uk/pdbsum/4faa 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=4faa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4faa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4faa RCSB], [http://www.ebi.ac.uk/pdbsum/4faa PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/COX2_THET8 COX2_THET8]] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
==See Also==
==See Also==

Revision as of 10:31, 25 December 2014

Structure of Recombinant Cytochrome ba3 Oxidase mutant A120F+A204F from Thermus thermophilus

4faa, resolution 2.80Å

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