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2lln
From Proteopedia
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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=2lln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lln RCSB], [http://www.ebi.ac.uk/pdbsum/2lln 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=2lln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lln RCSB], [http://www.ebi.ac.uk/pdbsum/2lln PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/COX2_THETH COX2_THETH]] 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 14:01, 25 December 2014
Solution structure of Thermus thermophilus apo-CuA
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