3oig

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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=3oig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oig RCSB], [http://www.ebi.ac.uk/pdbsum/3oig 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=3oig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oig RCSB], [http://www.ebi.ac.uk/pdbsum/3oig PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/FABI_BACSU FABI_BACSU]] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism.<ref>PMID:11007778</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 04:52, 25 December 2014

Crystal Structure of Enoyl-ACP Reductases I (FabI) from B. subtilis (complex with NAD and INH)

3oig, resolution 1.25Å

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