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3i8p

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==Crystal structure of E. coli FabF(C163A) in complex with Platensimycin A1==
==Crystal structure of E. coli FabF(C163A) in complex with Platensimycin A1==
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<StructureSection load='3i8p' size='340' side='right' caption='[[3i8p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3i8p' size='340' side='right'caption='[[3i8p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3i8p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I8P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3i8p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I8P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=840:PLATENSIMYCIN+A1'>840</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabF, fabJ, b1095, JW1081 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=840:PLATENSIMYCIN+A1'>840</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_II Beta-ketoacyl-acyl-carrier-protein synthase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.179 2.3.1.179] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8p OCA], [https://pdbe.org/3i8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i8p RCSB], [https://www.ebi.ac.uk/pdbsum/3i8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i8p ProSAT]</span></td></tr>
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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=3i8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i8p RCSB], [http://www.ebi.ac.uk/pdbsum/3i8p PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABF_ECOLI FABF_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i8/3i8p_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i8/3i8p_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3i8p ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3i8p" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase II]]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Parthsarathy, G]]
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[[Category: Parthsarathy G]]
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[[Category: Soisson, S M]]
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[[Category: Soisson SM]]
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[[Category: Acyltransferase]]
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[[Category: Fabf]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Kasii]]
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[[Category: Lipid synthesis]]
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[[Category: Platensimycin]]
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[[Category: Platensimycin a1]]
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[[Category: Transferase]]
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Current revision

Crystal structure of E. coli FabF(C163A) in complex with Platensimycin A1

PDB ID 3i8p

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