Structure of PDB 1qti Chain A

Receptor sequence
>1qtiA (length=527) Species: 7787 (Tetronarce californica) [Search protein sequence]
SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKP
WSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPS
PRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAF
GFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG
ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLN
CNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPT
SLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFM
SGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP
LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLV
KELNYTAEEEALSRRIMHYWATFAKTGNPNESKWPLFTTKEQKFIDLNTE
PMKVHQRLRVQMCVFWNQFLPKLLNAT
3D structure
PDB1qti Three-dimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-Alzheimer drugs
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GNT A W84 G117 G118 Y121 E199 S200 F288 F290 F331 H440 W81 G114 G115 Y118 E196 S197 F285 F287 F328 H437 PDBbind-CN: -logKd/Ki=6.44,IC50=0.36uM
BindingDB: IC50=1069nM,Ki=1.9e+2nM
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:1qti, PDBe:1qti, PDBj:1qti
PDBsum1qti
PubMed11119642
UniProtP04058|ACES_TETCF Acetylcholinesterase (Gene Name=ache)

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