4x0o

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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=4x0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x0o RCSB], [http://www.ebi.ac.uk/pdbsum/4x0o 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=4x0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x0o RCSB], [http://www.ebi.ac.uk/pdbsum/4x0o PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FABH2_VIBCH FABH2_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.[HAMAP-Rule:MF_01815]
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</StructureSection>
</StructureSection>

Revision as of 01:06, 25 December 2014

Beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae soaked with Acetyl-CoA

4x0o, resolution 2.20Å

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