Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004806 | molecular_function | triglyceride lipase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006629 | biological_process | lipid metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016298 | molecular_function | lipase activity |
A | 0016787 | molecular_function | hydrolase activity |
B | 0004806 | molecular_function | triglyceride lipase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0006629 | biological_process | lipid metabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016298 | molecular_function | lipase activity |
B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 182 |
Chain | Residue |
A | ILE12 |
A | SER77 |
A | MET78 |
A | HOH272 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 183 |
Chain | Residue |
A | TRP42 |
A | VAL54 |
A | ARG57 |
A | HOH246 |
A | HOH360 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 184 |
Chain | Residue |
A | MET137 |
A | ASN138 |
A | CYS139 |
A | ARG142 |
B | ARG107 |
B | HOH264 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 185 |
Chain | Residue |
A | ARG107 |
A | ASP144 |
B | ARG142 |
B | HOH309 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 186 |
Chain | Residue |
A | SER162 |
A | SER163 |
A | GLN164 |
A | HOH201 |
A | HOH477 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 182 |
Chain | Residue |
B | ILE12 |
B | SER77 |
B | MET78 |
B | HOH314 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 183 |
Chain | Residue |
B | TRP42 |
B | ARG57 |
B | HOH240 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 184 |
Chain | Residue |
B | SER162 |
B | SER163 |
B | GLN164 |
B | HOH371 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 185 |
Chain | Residue |
B | ILE135 |
B | HOH209 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER77 | |
B | SER77 | |
Chain | Residue | Details |
A | ASP133 | |
A | HIS156 | |
B | ASP133 | |
B | HIS156 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 518 |
Chain | Residue | Details |
A | ILE12 | electrostatic stabiliser |
A | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | MET78 | electrostatic stabiliser |
A | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
A | HIS156 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 518 |
Chain | Residue | Details |
B | ILE12 | electrostatic stabiliser |
B | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
B | MET78 | electrostatic stabiliser |
B | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
B | HIS156 | proton acceptor, proton donor |