Structure of PDB 5ehq Chain B

Receptor sequence
>5ehqB (length=537) Species: 10090 (Mus musculus) [Search protein sequence]
REDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEP
KRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVW
TPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYR
VGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGE
SAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLA
RLVGCPPGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGD
FLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISR
AQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHN
VVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFG
LPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTA
AQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSAT
3D structure
PDB5ehq Steric and Dynamic Parameters Influencing In Situ Cycloadditions to Form Triazole Inhibitors with Crystalline Acetylcholinesterase.
ChainB
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) G121 G122 G154 S203 A204 G242 F297 F299 E334 H447
Catalytic site (residue number reindexed from 1) G119 G120 G152 S201 A202 G240 F291 F293 E328 H441
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 5O2 B Y72 W86 Y124 E202 W286 Y337 Y341 W439 H447 Y449 Y70 W84 Y122 E200 W280 Y331 Y335 W433 H441 Y443 MOAD: Ki=33pM
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:5ehq, PDBe:5ehq, PDBj:5ehq
PDBsum5ehq
PubMed26731630
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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