1HPL
HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004465 | molecular_function | lipoprotein lipase activity |
| A | 0004806 | molecular_function | triacylglycerol lipase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008970 | molecular_function | phospholipase A1 activity |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019433 | biological_process | triglyceride catabolic process |
| A | 0034375 | biological_process | high-density lipoprotein particle remodeling |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047376 | molecular_function | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0004465 | molecular_function | lipoprotein lipase activity |
| B | 0004806 | molecular_function | triacylglycerol lipase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008970 | molecular_function | phospholipase A1 activity |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019433 | biological_process | triglyceride catabolic process |
| B | 0034375 | biological_process | high-density lipoprotein particle remodeling |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042632 | biological_process | cholesterol homeostasis |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047376 | molecular_function | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity |
| B | 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 960 |
| Chain | Residue |
| A | ASP195 |
| A | HOH1074 |
| A | HOH1261 |
| A | GLU187 |
| A | ARG190 |
| A | ASP192 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 970 |
| Chain | Residue |
| B | GLU187 |
| B | ARG190 |
| B | ASP192 |
| B | ASP195 |
| B | HOH1079 |
| B | HOH1162 |
| site_id | ACT |
| Number of Residues | 3 |
| Details | ACTIVE SITE IN CHAIN A |
| Chain | Residue |
| A | SER152 |
| A | ASP176 |
| A | HIS263 |
| site_id | BCT |
| Number of Residues | 3 |
| Details | ACTIVE SITE IN CHAIN B |
| Chain | Residue |
| B | SER152 |
| B | ASP176 |
| B | HIS263 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VHIIGHSLGS |
| Chain | Residue | Details |
| A | VAL146-SER155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 220 |
| Details | Domain: {"description":"PLAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00152","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 8182745, 9109604 |
| Chain | Residue | Details |
| A | HIS263 | |
| A | PHE77 | |
| A | ASP176 | |
| A | LEU153 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 8182745, 9109604 |
| Chain | Residue | Details |
| B | HIS263 | |
| B | PHE77 | |
| B | ASP176 | |
| B | LEU153 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 218 |
| Chain | Residue | Details |
| A | PHE77 | electrostatic stabiliser, hydrogen bond donor |
| A | SER152 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LEU153 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP176 | activator, hydrogen bond acceptor |
| A | HIS263 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 218 |
| Chain | Residue | Details |
| B | PHE77 | electrostatic stabiliser, hydrogen bond donor |
| B | SER152 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LEU153 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP176 | activator, hydrogen bond acceptor |
| B | HIS263 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
