6x7r
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with oxa(dethia)-coenzyme A== | |
| - | + | <StructureSection load='6x7r' size='340' side='right'caption='[[6x7r]], [[Resolution|resolution]] 1.35Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6x7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._DH10B Escherichia coli str. K-12 substr. DH10B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X7R 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]] 1.35Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UT7:oxa(dethia)-CoA'>UT7</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6x7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x7r OCA], [https://pdbe.org/6x7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x7r RCSB], [https://www.ebi.ac.uk/pdbsum/6x7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x7r ProSAT]</span></td></tr> |
| - | [[Category: Ling | + | </table> |
| - | [[Category: Lohman | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] 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. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815] |
| - | [[Category: Stunkard | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli str. K-12 substr. DH10B]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Benjamin AB]] | ||
| + | [[Category: Ling J]] | ||
| + | [[Category: Lohman JR]] | ||
| + | [[Category: Nice JN]] | ||
| + | [[Category: Stunkard LM]] | ||
Current revision
E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with oxa(dethia)-coenzyme A
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