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5zrn
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Inhibitor bound crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis== | |
| - | + | <StructureSection load='5zrn' size='340' side='right'caption='[[5zrn]], [[Resolution|resolution]] 2.37Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5zrn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZRN FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JSA:5-O-{[(1R)-1-hydroxydodecyl]sulfamoyl}adenosine'>JSA</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t5b|3t5b]]</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Long-chain-fatty-acid--CoA_ligase Long-chain-fatty-acid--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.3 6.2.1.3] </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=5zrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrn OCA], [http://pdbe.org/5zrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zrn RCSB], [http://www.ebi.ac.uk/pdbsum/5zrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FAC13_MYCTO FAC13_MYCTO]] 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 (By similarity). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Long-chain-fatty-acid--CoA ligase]] | ||
| + | [[Category: Goyal, A]] | ||
[[Category: Sankaranarayanan, R]] | [[Category: Sankaranarayanan, R]] | ||
| - | [[Category: | + | [[Category: Facl13]] |
| + | [[Category: Fatty acyl coa ligase]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Lipid metabolism]] | ||
| + | [[Category: Mycobacterium tuberculosis]] | ||
Revision as of 06:35, 24 April 2019
Inhibitor bound crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis
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