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 Cited by PubMed: 10673437DOI: 10.1016/S0969-2126(00)00094-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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