2QC1

Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0030550	molecular_function	acetylcholine receptor inhibitor activity
A	0035821	biological_process	modulation of process of another organism
A	0090729	molecular_function	toxin activity
A	0099106	molecular_function	ion channel regulator activity
B	0004888	molecular_function	transmembrane signaling receptor activity
B	0005216	molecular_function	monoatomic ion channel activity
B	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0022848	molecular_function	acetylcholine-gated monoatomic cation-selective channel activity
B	0034220	biological_process	monoatomic ion transmembrane transport
B	0045211	cellular_component	postsynaptic membrane

Functional Information from PROSITE/UniProt

site_id	PS00236
Number of Residues	15
Details	NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CeIiVthFPfDeqnC

Chain	Residue	Details
B	CYS128-CYS142

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site_id	PS00272
Number of Residues	21
Details	SNAKE_TOXIN Snake toxins signature. GCaatCPskkpyeevt.CCstD

Chain	Residue	Details
A	GLY43-ASP63

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	209
Details	Topological domain: {"description":"Extracellular"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17643119","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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