Structure of PDB 8aev Chain B Binding Site BS03

Receptor Information
>8aev Chain B (length=535) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQ
PWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTP
YPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVG
AFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESA
GAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHL
VGCPPGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFL
SDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAE
FLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVV
CPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIP
LDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQ
QYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSAT
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain8aev Chain B Residue 633 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8aev Grid-Type Quaternary Metallosupramolecular Compounds Inhibit Human Cholinesterases through Dynamic Multivalent Interactions.
Resolution2.89 Å
Binding residue
(original residue number in PDB)		S371 D372
Binding residue
(residue number reindexed from 1)		S363 D364
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
Gene Ontology
Molecular Function
GO:0001540 amyloid-beta binding
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:0001507 acetylcholine catabolic process in synaptic cleft
GO:0001919 regulation of receptor recycling
GO:0002076 osteoblast development
GO:0006581 acetylcholine catabolic process
GO:0007155 cell adhesion
GO:0007399 nervous system development
GO:0007416 synapse assembly
GO:0031623 receptor internalization
GO:0032223 negative regulation of synaptic transmission, cholinergic
GO:0042982 amyloid precursor protein metabolic process
GO:0050714 positive regulation of protein secretion
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:0005634 nucleus
GO:0005794 Golgi apparatus
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0031594 neuromuscular junction
GO:0043083 synaptic cleft
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:8aev, PDBe:8aev, PDBj:8aev
PDBsum8aev
PubMed36193860
UniProtP22303|ACES_HUMAN Acetylcholinesterase (Gene Name=ACHE)

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