4x9o: Difference between revisions

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'''Unreleased structure'''
==Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae soaked with octanoyl-CoA: conformational changes without clearly bound substrate==
 
<StructureSection load='4x9o' size='340' side='right' caption='[[4x9o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
The entry 4x9o is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4x9o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X9O FirstGlance]. <br>
Authors: Hou, J., Cooper, D.R., Grabowski, M., Shumilin, I., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID)
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wzu|4wzu]], [[4x0o|4x0o]], [[4x9k|4x9k]]</td></tr>
 
<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_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </span></td></tr>
Description: Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae soaked with octanoyl-CoA: conformational changes without clearly bound substrate
<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=4x9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x9o RCSB], [http://www.ebi.ac.uk/pdbsum/4x9o PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
== Function ==
[[http://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]
__TOC__
</StructureSection>
[[Category: Anderson, W F]]
[[Category: Structural genomic]]
[[Category: Cooper, D R]]
[[Category: Grabowski, M]]
[[Category: Hou, J]]
[[Category: Minor, W]]
[[Category: Minor, W]]
[[Category: Shabalin, I G]]
[[Category: Shumilin, I]]
[[Category: Shumilin, I]]
[[Category: Hou, J]]
[[Category: Beta-ketoacyl-acyl carrier protein synthase iii]]
[[Category: Anderson, W.F]]
[[Category: Csgid]]
[[Category: Grabowski, M]]
[[Category: Fabh]]
[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
[[Category: Transferase]]
[[Category: Cooper, D.R]]
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