6x7r: Difference between revisions
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== Structural highlights == | == 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> | <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='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> | </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> | ||
<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> | |||
<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> | <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> | ||
</table> | </table> | ||
Latest revision as of 12:16, 25 October 2023
E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with oxa(dethia)-coenzyme AE. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with oxa(dethia)-coenzyme A
Structural highlights
FunctionFABH_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] |
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