Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004806 | molecular_function | triacylglycerol lipase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 320 |
| Chain | Residue |
| A | ASP241 |
| A | ASP287 |
| A | GLN291 |
| A | LEU292 |
| A | VAL295 |
| A | HOH406 |
| A | HOH555 |
| site_id | ACT |
| Number of Residues | 3 |
| Details | THE CATALYTIC TRIAD OF THE ACTIVE CENTER CONSISTS OF THE RESIDUES SER 87 - HIS 285 - ASP 263, ALTHOUGH THEY ARE NOT EXPOSED TO THE SOLVENT, BUT A NARROW CHANNEL CONNECTS THEM WITH THE SURFACE. |
| Chain | Residue |
| A | SER87 |
| A | HIS285 |
| A | ASP263 |
| site_id | CA |
| Number of Residues | 6 |
| Details | CA BINDING SITE. |
| Chain | Residue |
| A | ASP241 |
| A | ASP287 |
| A | GLN291 |
| A | VAL295 |
| A | HOH460 |
| A | HOH555 |
| site_id | OXY |
| Number of Residues | 2 |
| Details | PERFORMED OXYANION, STABILIZED BY THE AMIDE NITROGEN ATOMS OF LEU 17 AND GLN 88, ALREADY PRESENT IN CLOSED CONFORMATION OF THE LIPASE. |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VNLIGHSQGG |
| Chain | Residue | Details |
| A | VAL81-GLY90 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"8683577","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"8683577","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22088","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8683577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGE","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| A | HIS285 | |
| A | SER87 | |
| A | ASP263 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| A | LEU17 | |
| A | HIS285 | |
| A | GLN88 | |
| A | SER87 | |
| A | ASP263 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
| A | ASP56 | electrostatic stabiliser |
| A | VAL126 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LEU127 | electrostatic stabiliser |
| A | SER280 | metal ligand |
| A | ASP302 | electrostatic stabiliser, increase basicity, modifies pKa |
