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451c

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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=451c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=451c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=451c RCSB], [http://www.ebi.ac.uk/pdbsum/451c 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=451c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=451c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=451c RCSB], [http://www.ebi.ac.uk/pdbsum/451c PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CY551_PSEAE CY551_PSEAE]] Electron donor for cytochrome cd1 in nitrite and nitrate respiration.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 11:38, 25 December 2014

STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS

451c, resolution 1.60Å

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