Structure of PDB 5nau Chain A Binding Site BS01

Receptor Information
>5nau Chain A (length=532) Species: 7787 (Tetronarce californica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKP
WSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPS
PRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAF
GFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG
ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLN
CNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPT
SLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFM
SGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP
LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLV
KELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFI
DLNTEPMKVHQRLRVQMCVFWNQFLPKLLNAT
Ligand information
Ligand IDDZ0
InChIInChI=1S/C23H25NO2/c1-26-21-7-8-22-19(15-21)14-20(23(22)25)13-17-9-11-24(12-10-17)16-18-5-3-2-4-6-18/h2-8,13,15,17H,9-12,14,16H2,1H3/b20-13+
InChIKeyCNIWTTNRVIMZIP-DEDYPNTBSA-N
SMILES
SoftwareSMILES
CACTVS 3.385COc1ccc2c(CC(=CC3CCN(CC3)Cc4ccccc4)C2=O)c1
OpenEye OEToolkits 2.0.6COc1ccc2c(c1)CC(=CC3CCN(CC3)Cc4ccccc4)C2=O
OpenEye OEToolkits 2.0.6COc1ccc2c(c1)C/C(=C\C3CCN(CC3)Cc4ccccc4)/C2=O
CACTVS 3.385COc1ccc2c(CC(=C/C3CCN(CC3)Cc4ccccc4)\C2=O)c1
FormulaC23 H25 N O2
Name(2~{E})-5-methoxy-2-[[1-(phenylmethyl)piperidin-4-yl]methylidene]-3~{H}-inden-1-one
ChEMBLCHEMBL3818084
DrugBank
ZINCZINC000137817655
PDB chain5nau Chain A Residue 611 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5nau Kinetic and structural studies on the interactions of Torpedo californica acetylcholinesterase with two donepezil-like rigid analogues.
Resolution2.25 Å
Binding residue
(original residue number in PDB)		W84 Y121 E199 W279 F330 F331 Y334 H440
Binding residue
(residue number reindexed from 1)		W81 Y118 E196 W276 F327 F328 Y331 H437
Annotation score1
Binding affinityMOAD: Ki=29.86nM
PDBbind-CN: -logKd/Ki=7.52,Kd=29.86nM
Enzymatic activity
Catalytic site (original residue number in PDB) G118 G119 G151 S200 A201 A239 F290 F292 E327 H440
Catalytic site (residue number reindexed from 1) G115 G116 G148 S197 A198 A236 F287 F289 E324 H437
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
Gene Ontology
Molecular Function
GO:0003990 acetylcholinesterase activity
GO:0004104 cholinesterase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0001507 acetylcholine catabolic process in synaptic cleft
GO:0006581 acetylcholine catabolic process
GO:0019695 choline metabolic process
Cellular Component
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0043083 synaptic cleft
GO:0045202 synapse
GO:0098552 side of membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5nau, PDBe:5nau, PDBj:5nau
PDBsum5nau
PubMed29651884
UniProtP04058|ACES_TETCF Acetylcholinesterase (Gene Name=ache)

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