Structure of PDB 5fkj Chain C Binding Site BS01

Receptor Information
>5fkj Chain C (length=536) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPK
RPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWT
PYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRV
GTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGES
AGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLAR
LVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVV
DGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESL
ISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVG
DHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEF
IFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPY
TTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKL
Ligand information
Ligand IDG0W
InChIInChI=1S/C37H56N6O6/c1-6-42(7-2,29-32-20-12-14-22-34(32)40(46)47)26-18-10-16-24-38-31(5)28-36(44)39(37(38)45)25-17-11-19-27-43(8-3,9-4)30-33-21-13-15-23-35(33)41(48)49/h12-15,20-23,28H,6-11,16-19,24-27,29-30H2,1-5H3/q+2
InChIKeyWLTAFWKKNBLBHO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC[N+](CC)(CCCCCN1C(=CC(=O)N(CCCCC[N+](CC)(CC)Cc2ccccc2[N+]([O-])=O)C1=O)C)Cc3ccccc3[N+]([O-])=O
OpenEye OEToolkits 1.7.6CC[N+](CC)(CCCCCN1C(=CC(=O)N(C1=O)CCCCC[N+](CC)(CC)Cc2ccccc2[N+](=O)[O-])C)Cc3ccccc3[N+](=O)[O-]
FormulaC37 H56 N6 O6
Name1,3-BIS[5(DIETHYL-O-NITROBENZYLAMMONIUM)PENTYL]-6-METHYLURACIL
ChEMBLCHEMBL3623902
DrugBank
ZINCZINC000150383719
PDB chain5fkj Chain C Residue 550 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5fkj Slow-Binding Inhibition of Acetylcholinesterase by a 6-Methyluracil Alkyl-Ammonium Derivative: Mechanism and Advantages for Myasthenia Gravis Treatment.
Resolution3.133 Å
Binding residue
(original residue number in PDB)		Y72 D74 W86 G121 Y124 S203 W286 H287 I294 F295 Y337 F338 Y341
Binding residue
(residue number reindexed from 1)		Y69 D71 W83 G118 Y121 S200 W283 H284 I291 F292 Y334 F335 Y338
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=10.66,Ki=22pM
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 F294 F296 E331 H444
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
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:5fkj, PDBe:5fkj, PDBj:5fkj
PDBsum5fkj
PubMed26929400
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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