Structure of PDB 5dtj Chain B

Receptor sequence
>5dtjB (length=532) Species: 10090 (Mus musculus) [Search protein sequence]
EDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPK
RPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWT
PYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRV
GTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGES
AGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLAR
LVGCPNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLS
DTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQF
LAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVC
PVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPL
DPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQ
YVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLS
3D structure
PDB5dtj Discovery of New Classes of Compounds that Reactivate Acetylcholinesterase Inhibited by Organophosphates.
ChainB
Resolution2.71 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) G118 G119 G151 S200 A201 G239 F288 F290 E325 H438
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 5G8 B Y72 Y124 S203 E285 W286 F295 R296 F338 N406 Y69 Y121 S200 E276 W277 F286 R287 F329 N397
BS02 5G8 B W86 Y124 S203 W286 F295 Y337 F338 Y341 H447 W83 Y121 S200 W277 F286 Y328 F329 Y332 H438
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:5dtj, PDBe:5dtj, PDBj:5dtj
PDBsum5dtj
PubMed26350723
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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