Structure of PDB 6wvq Chain A Binding Site BS01

Receptor Information

>6wvq Chain A (length=538) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

REDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEP
KQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVW
TPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYR
VGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGE
SAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLA
HLVGCPPTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVD
GDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLI
SRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGD
HNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFI
FGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYT
AGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSA

Ligand information

Ligand ID

UCY

InChI

InChI=1S/C8H17O2P/c1-8(2)6-4-5-7(8)10-11(3)9/h7,11H,4-6H2,1-3H3/t7-/m0/s1

InChIKey

GJIHMVVDUGLKHR-ZETCQYMHSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 2.0.7	CC1(CCCC1OP(=O)C)C
OpenEye OEToolkits 2.0.7	CC1(CCC[C@@H]1O[P@H](=O)C)C
CACTVS 3.385	C[PH](=O)O[CH]1CCCC1(C)C
CACTVS 3.385	C[P@H](=O)O[C@H]1CCCC1(C)C
ACDLabs 12.01	CP(=O)OC1C(C)(CCC1)C

Formula

C8 H17 O2 P

Name

(1S)-2,2-dimethylcyclopentyl (R)-methylphosphinate;
2,2-dimethylcyclopentyl methylphosphinate

ChEMBL

DrugBank

ZINC

PDB chain

6wvq Chain A Residue 606 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	6wvq Structural and Biochemical Insights into the Inhibition of Human Acetylcholinesterase by G-Series Nerve Agents and Subsequent Reactivation by HI-6.
Resolution	2.289 Å
Binding residue (original residue number in PDB)	W86 G121 G122 E202 S203 H447
Binding residue (residue number reindexed from 1)	W84 G119 G120 E200 S201 H443
Annotation score	1

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)	G119 G120 G152 S201 A202 G240 F293 F295 E330 H443
Enzyme Commision number	3.1.1.7: acetylcholinesterase.

Gene Ontology

	Molecular Function
GO:0001540	amyloid-beta binding
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:0001507	acetylcholine catabolic process in synaptic cleft
GO:0001919	regulation of receptor recycling
GO:0002076	osteoblast development
GO:0006581	acetylcholine catabolic process
GO:0007155	cell adhesion
GO:0007399	nervous system development
GO:0007416	synapse assembly
GO:0031623	receptor internalization
GO:0032223	negative regulation of synaptic transmission, cholinergic
GO:0042982	amyloid precursor protein metabolic process
GO:0050714	positive regulation of protein secretion
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:0005634	nucleus
GO:0005794	Golgi apparatus
GO:0005886	plasma membrane
GO:0009986	cell surface
GO:0016020	membrane
GO:0031594	neuromuscular junction
GO:0043083	synaptic cleft
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:6wvq, PDBe:6wvq, PDBj:6wvq
PDBsum	6wvq
PubMed	33538594
UniProt	P22303\|ACES_HUMAN Acetylcholinesterase (Gene Name=ACHE)

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