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[[Image:1hnd.png|left|200px]]


{{STRUCTURE_1hnd|  PDB=1hnd  |  SCENE=  }}
==CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX==
 
<StructureSection load='1hnd' size='340' side='right'caption='[[1hnd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
===CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1hnd]] is a 1 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=1HND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HND FirstGlance]. <br>
{{ABSTRACT_PUBMED_11243824}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnd OCA], [https://pdbe.org/1hnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hnd RCSB], [https://www.ebi.ac.uk/pdbsum/1hnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnd ProSAT]</span></td></tr>
[[1hnd]] 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=1HND OCA].  
</table>
== Function ==
[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]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hnd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1hnd ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:011243824</ref><references group="xtra"/>
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Head, M.]]
[[Category: Large Structures]]
[[Category: Janson, C A.]]
[[Category: Head M]]
[[Category: Konstantinidis, A K.]]
[[Category: Janson CA]]
[[Category: Lonsdale, J.]]
[[Category: Konstantinidis AK]]
[[Category: Qiu, X.]]
[[Category: Lonsdale J]]
[[Category: Smith, W W.]]
[[Category: Qiu X]]
[[Category: Fabh]]
[[Category: Smith WW]]
[[Category: Transferase]]

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