Structure of PDB 1lpa Chain B Binding Site BS01

Receptor Information
>1lpa 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 IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1lpa Chain B Residue 451 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lpa Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography.
Resolution3.04 Å
Binding residue
(original residue number in PDB)		E187 L188 R190 L191 D192 D195
Binding residue
(residue number reindexed from 1)		E188 L189 R191 L192 D193 D196
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:1lpa, PDBe:1lpa, PDBj:1lpa
PDBsum1lpa
PubMed8479519
UniProtP16233|LIPP_HUMAN Pancreatic triacylglycerol lipase (Gene Name=PNLIP)

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