Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004806 | molecular_function | triacylglycerol lipase activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 500 |
| Chain | Residue |
| A | GLU187 |
| A | ARG190 |
| A | ASP192 |
| A | ASP195 |
| A | HOH519 |
| A | HOH520 |
| site_id | CAT |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD. THE NUCLEOPHILE SER 152 IS LOCATED IN A BETA TURN AND HAS AN EPSILON CONFORMATION, COMMON FEATURE OF SERINE HYDROLASES. |
| Chain | Residue |
| A | SER152 |
| A | ASP176 |
| A | HIS263 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VHIIGHSLGA |
| Chain | Residue | Details |
| A | VAL146-ALA155 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | GLY167 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| A | LEU191 | |
| A | CYS296 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ILE202 | |
| A | ASP205 | |
| A | SER207 | |
| A | LEU210 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | TYR181 | |
| Chain | Residue | Details |
| A | SER152 | |
| Chain | Residue | Details |
| A | ASP176 | |
| A | HIS263 | |
| Chain | Residue | Details |
| A | GLU187 | |
| A | ARG190 | |
| A | ASP192 | |
| A | ASP195 | |
| Chain | Residue | Details |
| A | ASN334 | |
