1AKN
STRUCTURE OF BILE-SALT ACTIVATED LIPASE
Summary for 1AKN
| Entry DOI | 10.2210/pdb1akn/pdb |
| Descriptor | BILE-SALT ACTIVATED LIPASE, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | hydrolase, serine esterase, lipid degradation, glycoprotein, carboxylic esterase, hydrolase() |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 63832.57 |
| Authors | |
| Primary citation | Wang, X.,Wang, C.S.,Tang, J.,Dyda, F.,Zhang, X.C. The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism. Structure, 5:1209-1218, 1997 Cited by PubMed Abstract: The intestinally located pancreatic enzyme, bile salt activated lipase (BAL), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in a requirement of bile salts for activity. A structure-based explanation for these unique properties has not been reached so far due to the absence of a three-dimensional structure. PubMed: 9331420DOI: 10.1016/S0969-2126(97)00271-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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