Structure of PDB 1q83 Chain B

Receptor sequence
>1q83B (length=531) Species: 10090 (Mus musculus) [Search protein sequence]
EDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPK
RPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWT
PYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRV
GTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGES
AGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLAR
LVGCPNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLS
DTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQF
LAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVC
PVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPL
DPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQ
YVSLNLKPLEVRRGLRAQTCAFWNRFLPKLL
3D structure
PDB1q83 Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
ChainB
Resolution2.65 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 TZ5 B Y72 W86 G121 Y124 E202 W286 Y337 Y341 W439 H447 Y449 Y69 W83 G118 Y121 E199 W277 Y328 Y332 W430 H438 Y440 BindingDB: Ki=0.410nM,Kd=0.00041nM
Gene Ontology
Molecular Function
GO:0004104 cholinesterase activity

View graph for
Molecular Function
External links
PDB RCSB:1q83, PDBe:1q83, PDBj:1q83
PDBsum1q83
PubMed14757816
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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