4wzu
From Proteopedia
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==Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae== | ==Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae== | ||
<StructureSection load='4wzu' size='340' side='right' caption='[[4wzu]], [[Resolution|resolution]] 1.88Å' scene=''> | <StructureSection load='4wzu' size='340' side='right' caption='[[4wzu]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4wzu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wzu]] 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=4WZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZU FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=NA:SODIUM+ION'>NA</scene></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=4wzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzu OCA], [http://pdbe.org/4wzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wzu RCSB], [http://www.ebi.ac.uk/pdbsum/4wzu 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=4wzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzu OCA], [http://pdbe.org/4wzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wzu RCSB], [http://www.ebi.ac.uk/pdbsum/4wzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzu 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] | ||
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| - | ==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 12:14, 6 November 2017
Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae
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Categories: Vibch | Anderson, W F | Structural genomic | Chordia, M D | Chruszcz, M | Cooper, D R | Hou, J | Minor, W | Zheng, H | Zimmerman, M D | Csgid | Fabh | Transferase
