Structure of PDB 5dtj Chain A Binding Site BS02

Receptor Information
>5dtj Chain A (length=537) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DPMEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRF
MPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCL
YLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLV
SMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSV
TLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRR
ATLLARLVGCPNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVV
DGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESL
ISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVG
DHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEF
IFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPY
TTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLL
Ligand information
Ligand ID5G8
InChIInChI=1S/C14H16Cl2N2O/c15-12-4-5-14(13(16)10-12)19-9-3-1-2-7-18-8-6-17-11-18/h4-6,8,10-11H,1-3,7,9H2
InChIKeyRCLGZIGOWPMCRV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.9.2c1cc(c(cc1Cl)Cl)OCCCCCn2ccnc2
ACDLabs 12.01c2(OCCCCCn1ccnc1)c(Cl)cc(cc2)Cl
CACTVS 3.385Clc1ccc(OCCCCCn2ccnc2)c(Cl)c1
FormulaC14 H16 Cl2 N2 O
Name1-[5-(2,4-dichlorophenoxy)pentyl]-1H-imidazole
ChEMBL
DrugBank
ZINCZINC000002898719
PDB chain5dtj Chain A Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5dtj Discovery of New Classes of Compounds that Reactivate Acetylcholinesterase Inhibited by Organophosphates.
Resolution2.71 Å
Binding residue
(original residue number in PDB)		Y72 Y124 S203 E285 W286 F295 F297 F338 N406
Binding residue
(residue number reindexed from 1)		Y75 Y127 S206 E282 W283 F292 F294 F335 N403
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=4.47,Kd=34uM
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) G124 G125 G157 S206 A207 G245 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5dtj, PDBe:5dtj, PDBj:5dtj
PDBsum5dtj
PubMed26350723
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

[Back to BioLiP]