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 | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004806 | molecular_function | triglyceride lipase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | VAL296 |
| A | HOH507 |
| A | HOH538 |
| A | ASP242 |
| A | ASP288 |
| A | GLN292 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | ASP242 |
| B | ASP288 |
| B | GLN292 |
| B | VAL296 |
| B | HOH705 |
| B | HOH736 |
| site_id | ACT |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD. |
| Chain | Residue |
| A | SER87 |
| A | HIS286 |
| A | ASP264 |
| site_id | BCT |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD. |
| Chain | Residue |
| B | SER87 |
| B | HIS286 |
| B | ASP264 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VNLVGHSQGG |
| Chain | Residue | Details |
| A | VAL81-GLY90 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:15850979, ECO:0000305|PubMed:18386861, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP |
| Chain | Residue | Details |
| A | SER87 | |
| B | SER87 | |
| Chain | Residue | Details |
| A | ASP264 | |
| A | HIS286 | |
| B | ASP264 | |
| B | HIS286 | |
| Chain | Residue | Details |
| A | LEU17 | |
| A | GLN88 | |
| B | LEU17 | |
| B | GLN88 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP |
| Chain | Residue | Details |
| A | ASP242 | |
| A | ASP288 | |
| A | GLN292 | |
| A | VAL296 | |
| B | ASP242 | |
| B | ASP288 | |
| B | GLN292 | |
| B | VAL296 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| A | ASP264 | |
| A | HIS286 | |
| A | SER87 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| B | ASP264 | |
| B | HIS286 | |
| B | SER87 | |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| A | ASP264 | |
| A | HIS286 | |
| A | LEU17 | |
| A | GLN88 | |
| A | SER87 | |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| B | ASP264 | |
| B | HIS286 | |
| B | LEU17 | |
| B | GLN88 | |
| B | SER87 | |
