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1ebl

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{{Seed}}
 
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[[Image:1ebl.png|left|200px]]
 
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==THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI==
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The line below this paragraph, containing "STRUCTURE_1ebl", creates the "Structure Box" on the page.
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<StructureSection load='1ebl' size='340' side='right'caption='[[1ebl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ebl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EBL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#8491;</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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1ebl| PDB=1ebl | SCENE= }}
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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=1ebl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebl OCA], [https://pdbe.org/1ebl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ebl RCSB], [https://www.ebi.ac.uk/pdbsum/1ebl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ebl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/1ebl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1ebl ConSurf].
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<div style="clear:both"></div>
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===THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI===
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==See Also==
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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__TOC__
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</StructureSection>
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The line below this paragraph, {{ABSTRACT_PUBMED_10673437}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10673437 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10673437}}
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==About this Structure==
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1EBL is a [[Single protein]] structure of 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=1EBL OCA].
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==Reference==
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The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli., Davies C, Heath RJ, White SW, Rock CO, Structure. 2000 Feb 15;8(2):185-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10673437 10673437]
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Davies, C.]]
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[[Category: Davies C]]
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[[Category: Heath, R J.]]
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[[Category: Heath RJ]]
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[[Category: Rock, C O.]]
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[[Category: Rock CO]]
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[[Category: White, S W.]]
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[[Category: White SW]]
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[[Category: Acyltransferase]]
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[[Category: Alpha-beta protein]]
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[[Category: Coenzyme a binding protein]]
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[[Category: Condensing enzyme]]
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[[Category: Fatty acid synthesis]]
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[[Category: Five-layered fold]]
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[[Category: Helix dipole]]
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[[Category: Lipid metabolism]]
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[[Category: Malonyl coa decarboxylating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:27:29 2008''
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Current revision

THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI

PDB ID 1ebl

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