5hm3
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==2.25 Angstrom Resolution Crystal Structure of Long-chain-fatty-acid-AMP Ligase FadD32 from Mycobacterium tuberculosis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine== | |
| - | + | <StructureSection load='5hm3' size='340' side='right' caption='[[5hm3]], [[Resolution|resolution]] 2.25Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5hm3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HM3 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=649:5-O-[(11-PHENOXYUNDECANOYL)SULFAMOYL]ADENOSINE'>649</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5hm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hm3 OCA], [http://pdbe.org/5hm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hm3 RCSB], [http://www.ebi.ac.uk/pdbsum/5hm3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hm3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FAA32_MYCTU FAA32_MYCTU]] Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension.<ref>PMID:15042094</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aldrich, C C]] | ||
| + | [[Category: Anderson, W A]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Flores, K J]] | ||
| + | [[Category: Grimes, K D]] | ||
| + | [[Category: Kuhn, M L]] | ||
| + | [[Category: Minasov, G]] | ||
| + | [[Category: Shuvalova, L]] | ||
| + | [[Category: Warwrzak, Z]] | ||
| + | [[Category: Wilson, D J]] | ||
| + | [[Category: Csgid]] | ||
| + | [[Category: Fadd32]] | ||
| + | [[Category: Ligase-ligase inhibitor complex]] | ||
| + | [[Category: Long-chain-fatty-acid--amp ligase]] | ||
Revision as of 04:15, 4 August 2016
2.25 Angstrom Resolution Crystal Structure of Long-chain-fatty-acid-AMP Ligase FadD32 from Mycobacterium tuberculosis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine
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