Structure of PDB 2whp Chain A Binding Site BS01

Receptor Information
>2whp Chain A (length=531) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPP
EPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLN
VWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMN
YRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLF
GESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATL
LARLVGCNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDF
LSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRA
QFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNV
VCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGL
PLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPSPQWPPYTTAAQQYV
SLNLKPLEVRRGLRAQTCAFWNRFLPKLLSA
Ligand information
Ligand IDHI6
InChIInChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2
InChIKeyFJZDLOMCEPUCII-UHFFFAOYSA-P
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N
CACTVS 3.341NC(=O)c1cc[n+](COC[n+]2ccccc2C=NO)cc1
CACTVS 3.341NC(=O)c1cc[n+](COC[n+]2ccccc2\C=N\O)cc1
OpenEye OEToolkits 1.5.0c1cc[n+](c(c1)C=NO)COC[n+]2ccc(cc2)C(=O)N
ACDLabs 10.04O=C(N)c1cc[n+](cc1)COC[n+]2ccccc2\C=N\O
FormulaC14 H16 N4 O3
Name4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM;
1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-PYRIDINIUM DIMETHYLETHER
ChEMBLCHEMBL385181
DrugBank
ZINCZINC000000005077
PDB chain2whp Chain A Residue 1543 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2whp Structure of Hi-6Sarin-Acetylcholinesterase Determined by X-Ray Crystallography and Molecular Dynamics Simulation: Reactivator Mechanism and Design.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		Y124 X203 E285 W286 F297 S298 Y337 Y341
Binding residue
(residue number reindexed from 1)		Y124 X203 E278 W279 F290 S291 Y330 Y334
Annotation score1
Binding affinityMOAD: Kd~100uM
PDBbind-CN: -logKd/Ki=4.00,Kd=100uM
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) G121 G122 G154 S203 A204 G242 F290 F292 E327 H440
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
View graph for
Biological Process
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Cellular Component
External links
PDB RCSB:2whp, PDBe:2whp, PDBj:2whp
PDBsum2whp
PubMed19536291
UniProtP21836|ACES_MOUSE Acetylcholinesterase (Gene Name=Ache)

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