1aql Summary



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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A BILE-SALT ACTIVATED LIPASE P30122 (19-550) (CEL_BOVIN)search Bos taurussearch 92% 532 100%
B BILE-SALT ACTIVATED LIPASE P30122 (19-550) (CEL_BOVIN)search Bos taurussearch 92% 532 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P30122 (19 - 550) BILE-SALT ACTIVATED LIPASE Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P30122) Acetylcholinesterase-likesearch Rossmann foldsearch PF00135: Carboxylesterase familysearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B (P30122) sterol esterase activitysearch triglyceride lipase activitysearch hydrolase activitysearch carboxylic ester hydrolase activitysearch extracellular regionsearch cytoplasmsearch lipid metabolic processsearch lipid catabolic processsearch

Chain InterPro annotation
A, B Carboxylesterase, type Bsearch Carboxylesterase type B, conserved sitesearch Carboxylesterase type B, active sitesearch Alpha/Beta hydrolase foldsearch