1LPA
INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0005576 | cellular_component | extracellular region |
| A | 0007586 | biological_process | digestion |
| A | 0008047 | molecular_function | enzyme activator activity |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0035473 | molecular_function | lipase binding |
| A | 0043085 | biological_process | positive regulation of catalytic activity |
| B | 0001523 | biological_process | retinoid metabolic process |
| B | 0004465 | molecular_function | lipoprotein lipase activity |
| B | 0004806 | molecular_function | triacylglycerol lipase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008970 | molecular_function | glycerophospholipid phospholipase A1 activity |
| B | 0016298 | molecular_function | lipase 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 | 0044241 | biological_process | lipid digestion |
| B | 0047376 | molecular_function | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity |
| B | 0050253 | molecular_function | retinyl-palmitate esterase activity |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0061365 | biological_process | positive regulation of triglyceride lipase activity |
| B | 0120516 | molecular_function | diacylglycerol lipase activity |
Functional Information from PDB Data
| site_id | CAT |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| B | SER152 |
| B | ASP176 |
| B | HIS263 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 110 |
| Details | Domain: {"description":"PLAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00152","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P54317","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P54317","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7893686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8479519","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LPB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
