1AQL

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

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1aqla_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Acetylcholinesterase-like	Bile-salt activated lipase (cholesterol esterase)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B	d1aqlb_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Acetylcholinesterase-like	Bile-salt activated lipase (cholesterol esterase)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8032487	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032487	3000102	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00135	e1aqlA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00135	ECOD (1.6)
B	PF00135	e1aqlB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00135	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00135	Carboxylesterase family (COesterase)	Carboxylesterase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	BILE-SALT ACTIVATED LIPASE	hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity triglyceride lipase activity hydrolase activity catalytic activity lipase activity retinyl-palmitate esterase activity sterol esterase activity short-chain carboxylesterase activity acetylesterase activity	ceramide metabolic process membrane lipid metabolic process sphingolipid catabolic process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process lipid catabolic process cellular metabolic process sphingolipid metabolic process primary metabolic process membrane lipid catabolic process cellular lipid catabolic process cellular catabolic process organic substance metabolic process ceramide catabolic process ceramide metabolic process membrane lipid metabolic process sphingolipid catabolic process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process lipid catabolic process cellular metabolic process sphingolipid metabolic process primary metabolic process membrane lipid catabolic process cellular lipid catabolic process cellular catabolic process organic substance metabolic process ceramide catabolic process cellular lipid metabolic process metabolic process cellular process amide metabolic process organic substance catabolic process lipid metabolic process multicellular organismal process regulation of body fluid levels system process secretion by tissue pancreatic juice secretion digestive system process secretion transport biological regulation establishment of localization body fluid secretion localization digestion regulation of biological quality	intracellular anatomical structure cytoplasm cellular anatomical entity extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR019819	Carboxylesterase type B, conserved site	Conserved Site
A, B	IPR019826	Carboxylesterase type B, active site	Active Site
A, B	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B	IPR002018	Carboxylesterase, type B	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM	Monotopic/peripheral	Alpha/Beta monotopic/peripheral	Alpha/beta-hydrolases	Acetylcholinesterase-like

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	bile salt-activated lipase M-CSA #401	Bile salt-activated lipase (BAL) is one of two lipases secreted from the vertebrate pancreas into the intestine for the digestion of fat. It also catalyses vitamin absorption. It acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides. In a few mammals, BAL is also present in the milk to facilitate fat absorption in infants. Because of its wide range of substrate reactivities, BAL has been documented with several different names, including pancreatic carboxylester lipase, pancreatic cholesterol esterase, triacylglycerol lipase and lysophospholipase. There is evidence to support the importance of BAL for the absorption of cholesterol, vitamin A and triacylglycerol. The hydrolytic activity of BAL on naturally occurring lipids requires the presence of bile salt.	Defined by 6 residues: GLY:A-107ALA:A-108SER:A-194ALA:A-195ASP:A-320HIS:A-435 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.1.13 (PDB Primary Data) Search M-CSA Motif + EC 3.1.1.13

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.