Structure of PDB 1eth Chain C Binding Site BS04

Receptor Information
>1eth Chain C (length=448) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNY
QELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESV
NCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVI
GHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFV
DVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDID
GIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPC
PSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGK
KVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSDEFDSDVEVGDLQKVK
FIWYNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLNPC
Ligand information
Ligand IDC8E
InChIInChI=1S/C16H34O5/c1-2-3-4-5-6-7-9-18-11-13-20-15-16-21-14-12-19-10-8-17/h17H,2-16H2,1H3
InChIKeyFEOZZFHAVXYAMB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O(CCCCCCCC)CCOCCOCCOCCO
CACTVS 3.341
OpenEye OEToolkits 1.5.0		CCCCCCCCOCCOCCOCCOCCO
FormulaC16 H34 O5
Name(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
ChEMBL
DrugBankDB04233
ZINCZINC000014881140
PDB chain1eth Chain C Residue 456 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1eth Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		H76 G77 F78 I79 D80 W86 H152 S153 R257
Binding residue
(residue number reindexed from 1)		H76 G77 F78 I79 D80 W86 H152 S153 R257
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F78 S153 L154 D177 H264
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:0042572 retinol metabolic process
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:1eth, PDBe:1eth, PDBj:1eth
PDBsum1eth
PubMed8663362
UniProtP00591|LIPP_PIG Pancreatic triacylglycerol lipase (Gene Name=PNLIP)

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