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4wjz

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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=4wjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wjz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wjz RCSB], [http://www.ebi.ac.uk/pdbsum/4wjz 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=4wjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wjz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wjz RCSB], [http://www.ebi.ac.uk/pdbsum/4wjz PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FABG_VIBCH FABG_VIBCH]] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
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</StructureSection>
</StructureSection>

Revision as of 22:28, 25 December 2014

Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(G141A) from Vibrio cholerae

4wjz, resolution 2.40Å

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