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==Beta-ketoacyl-acyl carrier protein synthase III-2 (FabH2)(C113A) from Vibrio cholerae==
==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=''>
<StructureSection load='4x9k' size='340' side='right' caption='[[4x9k]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[4x9k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. 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>
</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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wzu|4wzu]], [[4x9o|4x9o]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH2, VC_A0751 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</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>
<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://pdbe.org/4x9k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x9k RCSB], [http://www.ebi.ac.uk/pdbsum/4x9k PDBsum]</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://pdbe.org/4x9k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x9k RCSB], [http://www.ebi.ac.uk/pdbsum/4x9k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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]  
[[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]  
==See Also==
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibch]]
[[Category: Anderson, W F]]
[[Category: Anderson, W F]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 18:25, 15 November 2017

Beta-ketoacyl-acyl carrier protein synthase III-2 (FabH2)(C113A) from Vibrio choleraeBeta-ketoacyl-acyl carrier protein synthase III-2 (FabH2)(C113A) from Vibrio cholerae

Structural highlights

4x9k is a 1 chain structure with sequence from Vibch. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:fabH2, VC_A0751 (VIBCH)
Activity:[acyl-carrier-protein_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number 2.3.1.180
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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]

4x9k, resolution 1.61Å

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OCA