4jrh

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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=4jrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jrh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jrh RCSB], [http://www.ebi.ac.uk/pdbsum/4jrh 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=4jrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jrh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jrh RCSB], [http://www.ebi.ac.uk/pdbsum/4jrh PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FABF_VIBCH FABF_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis (By similarity).
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</StructureSection>
</StructureSection>

Revision as of 22:23, 25 December 2014

Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Vibrio Cholerae (space group P43) at 2.2 Angstrom

4jrh, resolution 2.20Å

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