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1N8S

Structure of the pancreatic lipase-colipase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0004465molecular_functionlipoprotein lipase activity
A0004806molecular_functiontriacylglycerol lipase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0008970molecular_functionphospholipase A1 activity
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0019433biological_processtriglyceride catabolic process
A0030299biological_processintestinal cholesterol absorption
A0034375biological_processhigh-density lipoprotein particle remodeling
A0042572biological_processretinol metabolic process
A0042632biological_processcholesterol homeostasis
A0046872molecular_functionmetal ion binding
A0047376molecular_functionall-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity
A0050253molecular_functionretinyl-palmitate esterase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
A0061365biological_processpositive regulation of triglyceride lipase activity
C0001523biological_processretinoid metabolic process
C0005576cellular_componentextracellular region
C0006629biological_processlipid metabolic process
C0007586biological_processdigestion
C0008047molecular_functionenzyme activator activity
C0009617biological_processresponse to bacterium
C0016042biological_processlipid catabolic process
C0032094biological_processresponse to food
C0035473molecular_functionlipase binding
C0043085biological_processpositive regulation of catalytic activity
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VHVIGHSLGA
ChainResidueDetails
AVAL146-ALA155

site_idPS00121
Number of Residues9
DetailsCOLIPASE_1 Colipase signature. YgvYYkCpC
ChainResidueDetails
CTYR555-CYS563

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues110
DetailsDomain: {"description":"PLAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00152","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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