1LPB

THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A C11 ALKYL PHOSPHONATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0007586	biological_process	digestion
A	0008047	molecular_function	enzyme activator activity
A	0009617	biological_process	response to bacterium
A	0016042	biological_process	lipid catabolic process
A	0032094	biological_process	response to food
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	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	0030299	biological_process	intestinal cholesterol absorption
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	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

Functional Information from PDB Data

site_id	CAT
Number of Residues	3
Details

Chain	Residue
B	SER152
B	ASP176
B	HIS263

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Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. VHVIGHSLGA

Chain	Residue	Details
B	VAL146-ALA155

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site_id	PS00121
Number of Residues	9
Details	COLIPASE_1 Colipase signature. YgvYYkCpC

Chain	Residue	Details
A	TYR55-CYS63

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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

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

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