4nhd: Difference between revisions

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'''Unreleased structure'''


The entry 4nhd is ON HOLD
==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A==
<StructureSection load='4nhd' size='340' side='right'caption='[[4nhd]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nhd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [https://pdbe.org/4nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [https://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH] 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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).


Authors: Hou, J., Zheng, H., Langner, K., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID)
==See Also==
 
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
Description: Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Anderson WF]]
[[Category: Hou J]]
[[Category: Langner K]]
[[Category: Minor W]]
[[Category: Zheng H]]
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