CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE
The structure was published by Wang, X., Wang, C.S., Tang, J., Dyda, F., and Zhang, X.C., in 1997 in a paper entitled "The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1997.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of BILE-SALT ACTIVATED LIPASE.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: