4nmw: 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=4nmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nmw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nmw RCSB], [http://www.ebi.ac.uk/pdbsum/4nmw 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=4nmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nmw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nmw RCSB], [http://www.ebi.ac.uk/pdbsum/4nmw PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/BIOH_SALTY BIOH_SALTY]] The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters (By similarity).


==See Also==
==See Also==

Revision as of 05:34, 25 December 2014

Crystal Structure of Carboxylesterase BioH from Salmonella enterica

4nmw, resolution 1.50Å

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