Structure of PDB 6xyu Chain A Binding Site BS01

Receptor Information
>6xyu Chain A (length=537) Species: 7227 (Drosophila melanogaster) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEP
WHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPA
TTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFG
FLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFG
ESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEIGKAL
INDCNCNASMLKTNPAHVMSCMRSVDAKTISVQQWNSYSGILSFPSAPTI
DGAFLPADPMTLMKTADLKDYDILMGNVRDEGTYFLLYDFIDYFDKDDAT
ALPRDKYLEIMNNIFGKATQAEREAIIFQYTSWEGNPGYQNQQQIGRAVG
DHFFTCPTNEYAQALAERGASVHYYYFTHRTSTSLWGEWMGVLHGDEIEY
FFGQPLNNSLQYRPVERELGKRMLSAVIEFAKTGNPAQDGEEWPNFSKED
PVYYIFSTDDKIEKLARGPLAARCSFWNDYLPKVRSW
Ligand information
Ligand IDI40
InChIInChI=1S/C20H19IN2/c21-15-7-5-6-14(12-15)13-22-20-16-8-1-3-10-18(16)23-19-11-4-2-9-17(19)20/h1,3,5-8,10,12H,2,4,9,11,13H2,(H,22,23)
InChIKeyZUCWQTWGZGIYPV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04Ic1cccc(c1)CNc2c4c(nc3c2CCCC3)cccc4
CACTVS 3.341Ic1cccc(CNc2c3CCCCc3nc4ccccc24)c1
OpenEye OEToolkits 1.5.0c1ccc2c(c1)c(c3c(n2)CCCC3)NCc4cccc(c4)I
FormulaC20 H19 I N2
Name9-(3-IODOBENZYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE
ChEMBL
DrugBankDB07940
ZINCZINC000006583635
PDB chain6xyu Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6xyu A Second Look at the Crystal Structures ofDrosophila melanogasterAcetylcholinesterase in Complex with Tacrine Derivatives Provides Insights Concerning Catalytic Intermediates and the Design of Specific Insecticides.
Resolution2.51 Å
Binding residue
(original residue number in PDB)		Y71 W83 G150 G151 F330 Y370 W472
Binding residue
(residue number reindexed from 1)		Y69 W81 G114 G115 F294 Y334 W436
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G150 G151 S238 A239 E367 H480
Catalytic site (residue number reindexed from 1) G114 G115 S202 A203 E331 H444
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
Gene Ontology
Molecular Function
GO:0003990 acetylcholinesterase activity
GO:0004104 cholinesterase activity
GO:0008233 peptidase activity
GO:0017171 serine hydrolase activity
GO:0042803 protein homodimerization activity
GO:0043199 sulfate binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0001507 acetylcholine catabolic process in synaptic cleft
GO:0006581 acetylcholine catabolic process
GO:0007268 chemical synaptic transmission
GO:0019695 choline metabolic process
GO:0042426 choline catabolic process
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0043083 synaptic cleft
GO:0045202 synapse
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:6xyu, PDBe:6xyu, PDBj:6xyu
PDBsum6xyu
PubMed32155891
UniProtP07140|ACES_DROME Acetylcholinesterase (Gene Name=Ace)

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