3e53
From Proteopedia
(Difference between revisions)
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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=3e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e53 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e53 RCSB], [http://www.ebi.ac.uk/pdbsum/3e53 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=3e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e53 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e53 RCSB], [http://www.ebi.ac.uk/pdbsum/3e53 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/P96290_MYCTU P96290_MYCTU]] Catalyzes the activation of long-chain fatty acids (C22-24 fatty acids) as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase Mas for further chain extension. Involved in the biosynthesis of mycoserates (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 20:37, 24 December 2014
Crystal structure of N-terminal domain of a Fatty Acyl AMP Ligase FAAL28 from Mycobacterium tuberculosis
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