Structure of PDB 1maa Chain B Binding Site BS01

Receptor Information
>1maa Chain B (length=536) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
REDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEP
KRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVW
TPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYR
VGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGE
SAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLA
RLVGCNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLS
DTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQF
LAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVC
PVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPL
DPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDRKSPQWPPYTTAAQQ
YVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDT
Ligand information
Ligand IDDME
InChIInChI=1S/C16H38N2/c1-17(2,3)15-13-11-9-7-8-10-12-14-16-18(4,5)6/h7-16H2,1-6H3/q+2
InChIKeyMTCUAOILFDZKCO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341
OpenEye OEToolkits 1.5.0		C[N+](C)(C)CCCCCCCCCC[N+](C)(C)C
ACDLabs 10.04C(CCCC[N+](C)(C)C)CCCCC[N+](C)(C)C
FormulaC16 H38 N2
NameDECAMETHONIUM ION
ChEMBLCHEMBL1190
DrugBankDB01245
ZINCZINC000001532339
PDB chain1maa Chain B Residue 996 [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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PDB1maa Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		Y124 S293 I294 F338 Y341
Binding residue
(residue number reindexed from 1)		Y122 S284 I285 F329 Y332
Annotation score2
Binding affinityBindingDB: Ki=460nM
Enzymatic activity
Catalytic site (original residue number in PDB) G121 G122 G154 S203 A204 G242 F297 F299 E334 H447
Catalytic site (residue number reindexed from 1) G119 G120 G152 S201 A202 G240 F288 F290 E325 H438
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
Gene Ontology
Molecular Function
GO:0003990 acetylcholinesterase activity
GO:0004104 cholinesterase activity
GO:0005515 protein binding
GO:0005518 collagen binding
GO:0016787 hydrolase activity
GO:0017171 serine hydrolase activity
GO:0042166 acetylcholine binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043236 laminin binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0001919 regulation of receptor recycling
GO:0002076 osteoblast development
GO:0006581 acetylcholine catabolic process
GO:0007155 cell adhesion
GO:0031623 receptor internalization
GO:0060041 retina development in camera-type eye
GO:0095500 acetylcholine receptor signaling pathway
GO:0120162 positive regulation of cold-induced thermogenesis
Cellular Component
GO:0005576 extracellular region
GO:0005604 basement membrane
GO:0005615 extracellular space
GO:0005794 Golgi apparatus
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0031594 neuromuscular junction
GO:0045202 synapse
GO:0048471 perinuclear region of cytoplasm
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:1maa, PDBe:1maa, PDBj:1maa
PDBsum1maa
PubMed9915834
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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