2.3.1.221	additional information	domain architecture, the enzyme shows an alpha/beta-hydrolase fold in the catalytic closed form with a distinct hydrophobic substrate-binding chamber involving the PksA thioesterase/Claisen cyclase residues Ser1937, His2088, and Asp1964, which constitute the catalytic triad conserved in the alpha/beta-hydrolase family, detailed overview	723638	
2.3.1.221	additional information	domain organization of PksA with acyl-carrier protein (ACP), acyl transacylase (AT), dehydrase (DH), enoyl reductase (ER), ketoreductase (KR), ketoacyl synthase (KS), pseudomethyltransferase (PsiMT), starter unit:ACP transacylase (SAT), and thioesterase (TE), structure model, overview	723262	
2.3.1.221	additional information	domain structure, and dissection of domains, interactions, overview	721052	
2.3.1.221	additional information	PksA domain structure, from N- to C-terminus including the starter unit: acylcarrier protein transacylase (SAT), beta-ketoacyl synthase (KS), malonyl-CoA: acyl-carrier protein transacylase (MAT), product template (PT), acyl-carrier protein (ACP), and thioesterase/Claisen cyclase (TE/CLC)	722459