1AQL

CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE

Summary for 1AQL

• Entry DOI: 10.2210/pdb1aql/pdb
• Descriptor: BILE-SALT ACTIVATED LIPASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, TAUROCHOLIC ACID (3 entities in total)
• Functional Keywords: hydrolase, serine esterase, lipid degradation, glycoprotein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 2
• Total formula weight: 120636.15

Authors

Wang, X.,Zhang, X. (deposition date: 1997-07-30, release date: 1998-08-05, Last modification date: 2024-10-30)

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

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: 9331420
DOI: 10.1016/S0969-2126(97)00271-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)