1KAS
BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI
Summary for 1KAS
Entry DOI | 10.2210/pdb1kas/pdb |
Descriptor | BETA-KETOACYL ACP SYNTHASE II (2 entities in total) |
Functional Keywords | acyltransferase, condensing enzyme, fatty acid elongation, lipid metabolism, alpha-beta protein, five-layered fold, alpha-beta-alpha-beta-alpha |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 42958.43 |
Authors | Huang, W.,Jia, J.,Edwards, P.,Dehesh, K.,Schneider, G.,Lindqvist, Y. (deposition date: 1997-12-22, release date: 1999-03-02, Last modification date: 2024-02-07) |
Primary citation | Huang, W.,Jia, J.,Edwards, P.,Dehesh, K.,Schneider, G.,Lindqvist, Y. Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. EMBO J., 17:1183-1191, 1998 Cited by PubMed: 9482715DOI: 10.1093/emboj/17.5.1183 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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