Structure of PDB 2j3q Chain A Binding Site BS01

Receptor Information
>2j3q Chain A (length=533) 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
DLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATA
Ligand information
Ligand IDTFL
InChIInChI=1S/C16H16N2OS/c1-17(2)12-6-4-11(5-7-12)16-18(3)14-9-8-13(19)10-15(14)20-16/h4-10H,1-3H3/p+1
InChIKeyNOVJJPLRUMZSDK-UHFFFAOYSA-O
SMILES
SoftwareSMILES
ACDLabs 10.04Oc3ccc1c(sc([n+]1C)c2ccc(N(C)C)cc2)c3
CACTVS 3.341CN(C)c1ccc(cc1)c2sc3cc(O)ccc3[n+]2C
OpenEye OEToolkits 1.5.0C[n+]1c2ccc(cc2sc1c3ccc(cc3)N(C)C)O
FormulaC16 H17 N2 O S
Name2-[4-(DIMETHYLAMINO)PHENYL]-6-HYDROXY-3-METHYL-1,3-BENZOTHIAZOL-3-IUM
ChEMBL
DrugBankDB08615
ZINCZINC000038539054
PDB chain2j3q Chain A Residue 1538 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2j3q Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		Y70 Y121 W279 F330 F331 A536
Binding residue
(residue number reindexed from 1)		Y67 Y118 W276 F327 F328 A533
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=6.15,Kd=0.7uM
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:2j3q, PDBe:2j3q, PDBj:2j3q
PDBsum2j3q
PubMed18512913
UniProtP04058|ACES_TETCF Acetylcholinesterase (Gene Name=ache)

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