5kp2: Difference between revisions

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New page: '''Unreleased structure''' The entry 5kp2 is ON HOLD Authors: Hou, J., Zheng, H., Grabowski, M., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID)...
 
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'''Unreleased structure'''


The entry 5kp2 is ON HOLD
==Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae cocrystallized with octanoyl-CoA: hydrolzed ligand==
<StructureSection load='5kp2' size='340' side='right'caption='[[5kp2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kp2]] is a 2 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=5KP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KP2 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]] 2&#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>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</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=5kp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kp2 OCA], [https://pdbe.org/5kp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kp2 RCSB], [https://www.ebi.ac.uk/pdbsum/5kp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kp2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABH2_VIBCH FABH2_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.[HAMAP-Rule:MF_01815]


Authors: Hou, J., Zheng, H., Grabowski, M., 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: Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae soaked with octanoyl-CoA: hydrolzed ligand
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Zheng, H]]
[[Category: Large Structures]]
[[Category: Minor, W]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Hou, J]]
[[Category: Anderson WF]]
[[Category: Anderson, W.F]]
[[Category: Grabowski M]]
[[Category: Grabowski, M]]
[[Category: Hou J]]
[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
[[Category: Minor W]]
[[Category: Zheng H]]
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