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5JME

Crystal structure of acetylcholine binding protein (AChBP) from Aplysia Californica in complex with alpha-conotoxin PeIA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005216molecular_functionmonoatomic ion channel activity
A0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0004888molecular_functiontransmembrane signaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0004888molecular_functiontransmembrane signaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
D0004888molecular_functiontransmembrane signaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
F0005576cellular_componentextracellular region
F0030550molecular_functionacetylcholine receptor inhibitor activity
G0005576cellular_componentextracellular region
G0030550molecular_functionacetylcholine receptor inhibitor activity
H0005576cellular_componentextracellular region
H0030550molecular_functionacetylcholine receptor inhibitor activity
I0005576cellular_componentextracellular region
I0030550molecular_functionacetylcholine receptor inhibitor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI7
Number of Residues60
DetailsPeptide: {"description":"Alpha-conotoxin PeIA","featureId":"PRO_0000247851","evidences":[{"source":"PubMed","id":"15983035","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21252227","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsRegion: {"description":"Ser-Xaa-Pro motif, crucial for potent interaction with nAChR","evidences":[{"source":"UniProtKB","id":"P56636","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues16
DetailsSite: {"description":"Important residue for inhibiting alpha-3-beta-2 nAChR","evidences":[{"source":"PubMed","id":"23846688","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsSite: {"description":"Residue that is not optimum for the most potent inhibition of alpha-3-beta-2 and alpha-6/alpha-3-beta-2-beta-3 and alpha-6/alpha-3-beta-4","evidences":[{"source":"PubMed","id":"22914547","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23846688","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsSite: {"description":"Important residue for inhibiting alpha-3-beta-2 and alpha-6/alpha-3-beta-2-beta-3 nAChR","evidences":[{"source":"PubMed","id":"23846688","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Cysteine amide","evidences":[{"source":"PubMed","id":"15983035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2026-03-11

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