4QWW

Crystal structure of the Fab410-BfAChE complex

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
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005886	cellular_component	plasma membrane
A	0006581	biological_process	acetylcholine catabolic process
A	0019695	biological_process	choline metabolic process
A	0035821	biological_process	modulation of process of another organism
A	0043083	cellular_component	synaptic cleft
A	0045202	cellular_component	synapse
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	0090729	molecular_function	toxin activity
B	0001507	biological_process	acetylcholine catabolic process in synaptic cleft
B	0003990	molecular_function	acetylcholinesterase activity
B	0004104	molecular_function	cholinesterase activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005886	cellular_component	plasma membrane
B	0006581	biological_process	acetylcholine catabolic process
B	0019695	biological_process	choline metabolic process
B	0035821	biological_process	modulation of process of another organism
B	0043083	cellular_component	synaptic cleft
B	0045202	cellular_component	synapse
B	0052689	molecular_function	carboxylic ester hydrolase activity
B	0090729	molecular_function	toxin activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE187-GLY202

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH

Chain	Residue	Details
C	TYR191-HIS197

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

Chain	Residue	Details
A	GLU92-PRO102

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255\|PROSITE-ProRule:PRU10039

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Charge relay system => ECO:0000250

site_id	SWS_FT_FI3
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:25411244, ECO:0007744\|PDB:4QWW