Annotations: 1PQR

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1pqra_	Peptides	Conotoxins	Conotoxins	Alpha-a-conotoxin	Alpha-a-conotoxin eIVa	( ) [TaxId: ], (Conus ermineus ) [TaxId: 55423 ],	SCOPe (2.08)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF07829	Alpha-A conotoxin PIVA-like protein (Toxin_14)	Alpha-A conotoxin PIVA-like protein	Alpha-A conotoxin PIVA (Swiss:P55963) is the major paralytic toxin found in the venom produced by the piscivorous snail Conus purpurascens. This peptide acts by blocking the acetylcholine binding site of the nicotinic acetylcholine receptor at the ne ...	Alpha-A conotoxin PIVA (Swiss:P55963) is the major paralytic toxin found in the venom produced by the piscivorous snail Conus purpurascens. This peptide acts by blocking the acetylcholine binding site of the nicotinic acetylcholine receptor at the neuromuscular junction [1]. The overall shape of the peptide is described as an "iron" with a highly charged hydrophilic loop of 15S-19R forming the "handle" domain that is exposed to the exterior of the protein. The stability of the conotoxin is primarily governed by three disulphide bonds. A triangular structural motif formed by residues 19R, 12H and 6Y is thought to constitute a "binding core" that is important in binding to the acetylcholine receptor [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Alpha-A-conotoxin EIVA	passive transmembrane transporter activity channel regulator activity ion channel regulator activity monoatomic ion channel activity channel activity molecular function regulator activity monoatomic ion transmembrane transporter activity transporter activity transporter regulator activity transmembrane transporter activity neurotransmitter receptor regulator activity molecular transducer activity signaling receptor activity signaling receptor inhibitor activity passive transmembrane transporter activity channel regulator activity ion channel regulator activity monoatomic ion channel activity channel activity molecular function regulator activity monoatomic ion transmembrane transporter activity transporter activity transporter regulator activity transmembrane transporter activity neurotransmitter receptor regulator activity molecular transducer activity signaling receptor activity signaling receptor inhibitor activity neurotransmitter receptor activity acetylcholine receptor regulator activity molecular function inhibitor activity postsynaptic neurotransmitter receptor activity acetylcholine receptor inhibitor activity transmembrane signaling receptor activity signaling receptor regulator activity acetylcholine receptor activity toxin activity	-	cellular anatomical structure extracellular region host cellular component host cell part host cell postsynaptic membrane host cell membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR012498	Alpha-A conotoxin PIVA-like	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	HYP	Parent Component: PRO RESID: AA0030 PSI-MOD : 4-hydroxy-L-proline MOD:00039
A	NH2	RESID: AA0030 , AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 PSI-MOD : 4-hydroxy-L-proline MOD:00039 , L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.