Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004806 | molecular_function | triglyceride lipase activity |
A | 0005576 | cellular_component | extracellular region |
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 | 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 | 5 |
Details | binding site for residue CL A 201 |
Chain | Residue |
A | GLY155 |
A | HIS156 |
A | ILE157 |
A | GLY158 |
B | GLY155 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue BM0 A 202 |
Chain | Residue |
A | SER77 |
A | HIS156 |
A | HOH305 |
A | ILE12 |
A | GLY13 |
A | GLY14 |
A | ASN18 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue BM0 A 203 |
Chain | Residue |
A | TYR49 |
A | ASN50 |
A | HOH302 |
B | HIS3 |
B | LYS35 |
B | THR66 |
B | GLY67 |
B | ALA68 |
B | MET137 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue BM0 A 204 |
Chain | Residue |
A | THR45 |
A | THR47 |
A | HOH396 |
B | LEU108 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue BM0 A 205 |
Chain | Residue |
A | GLY116 |
A | ASP118 |
A | PRO119 |
A | LYS122 |
A | HOH375 |
B | HOH348 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue BM0 A 206 |
Chain | Residue |
A | ASP34 |
A | LEU36 |
A | TYR37 |
A | ARG107 |
A | ARG142 |
A | ASP144 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue CL B 201 |
Chain | Residue |
A | GLY155 |
A | HOH306 |
B | HIS156 |
B | ILE157 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CL B 202 |
Chain | Residue |
B | THR47 |
B | ASN48 |
B | HOH380 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue BM0 B 203 |
Chain | Residue |
A | ILE157 |
B | TRP42 |
B | GLY158 |
B | TYR161 |
B | HOH367 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue BM0 B 204 |
Chain | Residue |
B | ASP34 |
B | LEU36 |
B | TYR37 |
B | ARG107 |
B | ARG142 |
B | ASP144 |
B | HOH381 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue BM0 B 205 |
Chain | Residue |
A | TYR161 |
B | PHE17 |
B | TYR161 |
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 |