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4u0p

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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=4u0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u0p RCSB], [http://www.ebi.ac.uk/pdbsum/4u0p 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=4u0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u0p RCSB], [http://www.ebi.ac.uk/pdbsum/4u0p PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/LIPA2_THEEB LIPA2_THEEB]] Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 16:13, 24 December 2014

The Crystal Structure of Lipoyl Synthase in Complex with S-Adenosyl Homocysteine

4u0p, resolution 1.62Å

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