Structure of PDB 1lpb Chain B Binding Site BS02

Receptor Information
>1lpb Chain B (length=449) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTNENPNNF
QEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESV
NCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVI
GHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFV
DVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDID
GIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPC
PSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVSVTLSGK
KVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVK
FIWYNNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
Ligand information
Ligand IDMUP
InChIInChI=1S/C12H27O3P/c1-3-4-5-6-7-8-9-10-11-12-16(13,14)15-2/h3-12H2,1-2H3,(H,13,14)
InChIKeyJBVUSHKPEBKWQP-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(OC)CCCCCCCCCCC
OpenEye OEToolkits 1.5.0CCCCCCCCCCC[P@](=O)(O)OC
CACTVS 3.341CCCCCCCCCCC[P](O)(=O)OC
OpenEye OEToolkits 1.5.0CCCCCCCCCCCP(=O)(O)OC
CACTVS 3.341CCCCCCCCCCC[P@@](O)(=O)OC
FormulaC12 H27 O3 P
NameMETHOXYUNDECYLPHOSPHINIC ACID
ChEMBL
DrugBankDB08222
ZINCZINC000002043208
PDB chain1lpb Chain B Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lpb The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate.
Resolution2.46 Å
Binding residue
(original residue number in PDB)		G76 F77 S152 L153 A178 F215 H263
Binding residue
(residue number reindexed from 1)		G77 F78 S153 L154 A179 F216 H264
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F77 S152 L153 D176 H263
Catalytic site (residue number reindexed from 1) F78 S153 L154 D177 H264
Enzyme Commision number 3.1.1.3: triacylglycerol lipase.
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016298 lipase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047376 all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0016042 lipid catabolic process
GO:0030299 intestinal cholesterol absorption
GO:0042572 retinol metabolic process
GO:0061365 positive regulation of triglyceride lipase activity
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lpb, PDBe:1lpb, PDBj:1lpb
PDBsum1lpb
PubMed7893686
UniProtP16233|LIPP_HUMAN Pancreatic triacylglycerol lipase (Gene Name=PNLIP)

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