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8d1u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A== | |
| - | + | <StructureSection load='8d1u' size='340' side='right'caption='[[8d1u]], [[Resolution|resolution]] 1.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8d1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6x7s 6x7s]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D1U 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]] 1.302Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</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=8d1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d1u OCA], [https://pdbe.org/8d1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d1u RCSB], [https://www.ebi.ac.uk/pdbsum/8d1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d1u 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]] | ||
| + | [[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) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A
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