Structure of PDB 6wvo Chain B

Receptor sequence
>6wvoB (length=539) Species: 9606 (Homo sapiens) [Search protein sequence]
GREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPE
PKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNV
WTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNY
RVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFG
ESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQL
AHLVGCPPTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVV
DGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESL
ISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVG
DHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEF
IFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPY
TAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSA
3D structure
PDB6wvo Structural and Biochemical Insights into the Inhibition of Human Acetylcholinesterase by G-Series Nerve Agents and Subsequent Reactivation by HI-6.
ChainB
Resolution2.19 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) G120 G121 G153 S202 A203 G241 F294 F296 E331 H444
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 GD8 B W86 G121 G122 S203 A204 H447 W85 G120 G121 S202 A203 H444
BS02 HI6 B Y72 D74 Y124 V282 W286 Y337 Y341 Y71 D73 Y123 V279 W283 Y334 Y338 BindingDB: IC50=667800nM,Kd=93000nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6wvo, PDBe:6wvo, PDBj:6wvo
PDBsum6wvo
PubMed33538594
UniProtP22303|ACES_HUMAN Acetylcholinesterase (Gene Name=ACHE)

[Back to BioLiP]