4x9k: Difference between revisions

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-'''Unreleased structure'''
+==Beta-ketoacyl-acyl carrier protein synthase III-2 (FabH2)(C113A) from Vibrio cholerae==
+<StructureSection load='4x9k' size='340' side='right' caption='[[4x9k]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
-The entry 4x9k is ON HOLD
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4x9k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X9K FirstGlance]. <br>
-Authors: Hou, J
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wzu|4wzu]], [[4x9o|4x9o]]</td></tr>
-Description: Beta-ketoacyl-acyl carrier protein synthase III-2 (FabH2)(C113A) from Vibrio cholerae
+<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>
+<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=4x9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x9k RCSB], [http://www.ebi.ac.uk/pdbsum/4x9k PDBsum]</span></td></tr>
+</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: Structural genomic]]
+[[Category: Hou, J]]
+[[Category: Csgid]]
+[[Category: Fabh]]
+[[Category: Transferase]]