1EBL

THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI

Summary for 1EBL

• Entry DOI: 10.2210/pdb1ebl/pdb
• Related: 1D9B
• Descriptor: BETA-KETOACYL-ACP SYNTHASE III, COENZYME A (3 entities in total)
• Functional Keywords: acyltransferase, condensing enzyme, fatty acid synthesis, lipid metabolism, alpha-beta protein, five-layered fold, coenzyme a binding protein, helix dipole, malonyl coa decarboxylating enzyme, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6R0
• Total number of polymer chains: 2
• Total formula weight: 69381.33

Authors

Davies, C.,Heath, R.J.,White, S.W.,Rock, C.O. (deposition date: 2000-01-24, release date: 2000-02-11, Last modification date: 2018-01-31)

• Primary citation: Davies, C.,Heath, R.J.,White, S.W.,Rock, C.O.; The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.; Structure Fold.Des., 8:185-195, 2000; PubMed: 10673437; DOI: 10.1016/S0969-2126(00)00094-0

Experimental method

X-RAY DIFFRACTION (1.8 Å)