7AIX

Crystal structure of Torpedo Californica acetylcholinesterase in complex with 2-{1-[4-(12-Amino-3-chloro-6,7,10,11-tetrahydro-7,11-methanocycloocta[b]quinolin-9-yl)butyl]-1H-1,2,3-triazol-4-yl}-N-[4-hydroxy-3-methoxybenzyl]acetamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001507	biological_process	acetylcholine catabolic process in synaptic cleft
A	0003990	molecular_function	acetylcholinesterase activity
A	0004104	molecular_function	cholinesterase activity

Functional Information from PROSITE/UniProt

site_id	PS00122
Number of Residues	16
Details	CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG

Chain	Residue	Details
A	PHE187-GLY202

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site_id	PS00941
Number of Residues	11
Details	CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP

Chain	Residue	Details
A	GLU92-PRO102

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Acyl-ester intermediate

Chain	Residue	Details
A	SER200

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system

Chain	Residue	Details
A	GLU327
A	HIS440

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site_id	SWS_FT_FI3
Number of Residues	1
Details	LIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:8597567

Chain	Residue	Details
A	SER543

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558

Chain	Residue	Details
A	ASN59

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899

Chain	Residue	Details
A	ASN416

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site_id	SWS_FT_FI6
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299

Chain	Residue	Details
A	ASN457
A	ASN533

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