Structure of PDB 5eie Chain A

Receptor sequence
>5eieA (length=538) Species: 10090 (Mus musculus) [Search protein sequence]
EGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPP
EPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLN
VWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMN
YRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLF
GESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATL
LARLVGCPPNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDG
DFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLIS
RAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDH
NVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIF
GLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTT
AAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSAT
3D structure
PDB5eie Steric and Dynamic Parameters Influencing In Situ Cycloadditions to Form Triazole Inhibitors with Crystalline Acetylcholinesterase.
ChainA
Resolution2.1 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) G121 G122 G154 S203 A204 G242 F292 F294 E329 H442
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 TZ2 A W86 G121 Y124 E202 F297 Y337 W439 H447 Y449 W86 G121 Y124 E202 F292 Y332 W434 H442 Y444 MOAD: Ki=23000pM
PDBbind-CN: -logKd/Ki=7.64,Ki=23nM
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:5eie, PDBe:5eie, PDBj:5eie
PDBsum5eie
PubMed26731630
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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