4r8e

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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=4r8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8e RCSB], [http://www.ebi.ac.uk/pdbsum/4r8e 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=4r8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8e RCSB], [http://www.ebi.ac.uk/pdbsum/4r8e PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/Q7CJ22_YERPE Q7CJ22_YERPE]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.[PIRNR:PIRNR000447]
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</StructureSection>
</StructureSection>

Revision as of 18:56, 25 December 2014

Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Yersinia pestis

4r8e, resolution 2.70Å

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