3t5c

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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=3t5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t5c RCSB], [http://www.ebi.ac.uk/pdbsum/3t5c 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=3t5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t5c RCSB], [http://www.ebi.ac.uk/pdbsum/3t5c PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FAC13_MYCTU FAC13_MYCTU]] Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. It has preference for the fatty acid with long chain length in the following order: hexacosanoic acid (C26), tetracosanoic acid (C24) and palmitic acid (C16).<ref>PMID:15937179</ref> <ref>PMID:20027301</ref> <ref>PMID:22560731</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 13:37, 24 December 2014

Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2

3t5c, resolution 2.09Å

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