1AQL
CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004771 | molecular_function | sterol ester esterase activity |
A | 0004806 | molecular_function | triacylglycerol lipase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008126 | molecular_function | acetylesterase activity |
A | 0016020 | cellular_component | membrane |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030157 | biological_process | pancreatic juice secretion |
A | 0042572 | biological_process | retinol metabolic process |
A | 0046514 | biological_process | ceramide catabolic process |
A | 0050253 | molecular_function | retinyl-palmitate esterase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
B | 0004771 | molecular_function | sterol ester esterase activity |
B | 0004806 | molecular_function | triacylglycerol lipase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005737 | cellular_component | cytoplasm |
B | 0006629 | biological_process | lipid metabolic process |
B | 0008126 | molecular_function | acetylesterase activity |
B | 0016020 | cellular_component | membrane |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030157 | biological_process | pancreatic juice secretion |
B | 0042572 | biological_process | retinol metabolic process |
B | 0046514 | biological_process | ceramide catabolic process |
B | 0050253 | molecular_function | retinyl-palmitate esterase activity |
B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-ester intermediate |
Chain | Residue | Details |
A | SER194 | |
B | SER194 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | ASP320 | |
A | HIS435 | |
B | ASP320 | |
B | HIS435 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN187 | |
A | ASN361 | |
B | ASN187 | |
B | ASN361 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | a catalytic site defined by CSA, PubMed 9331420 |
Chain | Residue | Details |
A | SER194 | |
A | HIS435 | |
A | ASP320 | |
A | GLY107 | |
A | ALA108 | |
A | ALA195 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 401 |
Chain | Residue | Details |
A | GLY107 | electrostatic stabiliser |
A | ALA108 | electrostatic stabiliser |
A | SER194 | covalent catalysis |
A | ALA195 | electrostatic stabiliser |
A | ASP320 | activator, electrostatic stabiliser |
A | HIS435 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 401 |
Chain | Residue | Details |
B | GLY107 | electrostatic stabiliser |
B | ALA108 | electrostatic stabiliser |
B | SER194 | covalent catalysis |
B | ALA195 | electrostatic stabiliser |
B | ASP320 | activator, electrostatic stabiliser |
B | HIS435 | proton shuttle (general acid/base) |