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1c9e

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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=1c9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c9e RCSB], [http://www.ebi.ac.uk/pdbsum/1c9e 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=1c9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c9e RCSB], [http://www.ebi.ac.uk/pdbsum/1c9e PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HEMH_BACSU HEMH_BACSU]] Catalyzes the ferrous insertion into protoporphyrin IX.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 12:26, 25 December 2014

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

1c9e, resolution 2.30Å

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