Structure of PDB 4m0f Chain A

Receptor sequence
>4m0fA (length=530) Species: 9606 (Homo sapiens) [Search protein sequence]
EDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPK
QPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWT
PYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRV
GAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGES
AGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAH
LVGCPNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLS
DTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEF
LAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVC
PVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPL
DPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPQWPPYTAGAQQYVS
LDLRPLEVRRGLRAQACAFWNRFLPKLLSA
3D structure
PDB4m0f Structures of human acetylcholinesterase bound to dihydrotanshinone I and territrem B show peripheral site flexibility.
ChainA
Resolution2.304 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 1YK A W86 Y124 W286 Y337 F338 Y341 H447 W83 Y121 W277 Y328 F329 Y332 H438 MOAD: Ki=1.7nM
PDBbind-CN: -logKd/Ki=8.77,Ki=1.7nM
BindingDB: Ki=1.7nM,IC50=8nM
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
View graph for
Biological Process
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Cellular Component
External links
PDB RCSB:4m0f, PDBe:4m0f, PDBj:4m0f
PDBsum4m0f
PubMed24900610
UniProtP22303|ACES_HUMAN Acetylcholinesterase (Gene Name=ACHE)

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