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●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

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 ID C8E InChI InChI=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 InChIKey FEOZZFHAVXYAMB-UHFFFAOYSA-N SMILES Software SMILES ACDLabs 10.04 O(CCCCCCCC)CCOCCOCCOCCO CACTVS 3.341 OpenEye OEToolkits 1.5.0 CCCCCCCCOCCOCCOCCOCCO Formula C16 H34 O5 Name (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE ChEMBL DrugBank DB04233 ZINC ZINC000014881140 PDB chain 1eth Chain C Residue 456 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1eth Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. Resolution 2.8 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 score 1

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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