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7CFT

Cryo-EM strucutre of human acid-sensing ion channel 1a in complex with snake toxin Mambalgin1 at pH 8.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0005272molecular_functionsodium channel activity
A0006814biological_processsodium ion transport
A0015280molecular_functionligand-gated sodium channel activity
A0016020cellular_componentmembrane
B0005272molecular_functionsodium channel activity
B0006814biological_processsodium ion transport
B0015280molecular_functionligand-gated sodium channel activity
B0016020cellular_componentmembrane
C0005272molecular_functionsodium channel activity
C0006814biological_processsodium ion transport
C0015280molecular_functionligand-gated sodium channel activity
C0016020cellular_componentmembrane
D0005576cellular_componentextracellular region
D0035821biological_processmodulation of process of another organism
D0090729molecular_functiontoxin activity
D0099106molecular_functionion channel regulator activity
E0005576cellular_componentextracellular region
E0035821biological_processmodulation of process of another organism
E0090729molecular_functiontoxin activity
E0099106molecular_functionion channel regulator activity
F0005576cellular_componentextracellular region
F0035821biological_processmodulation of process of another organism
F0090729molecular_functiontoxin activity
F0099106molecular_functionion channel regulator activity
Functional Information from PROSITE/UniProt
site_idPS01206
Number of Residues21
DetailsASC Amiloride-sensitive sodium channels signature. YsiTaCridCeTryLVenCnC
ChainResidueDetails
ATYR305-CYS325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"34319232","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7RNN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1080
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34319232","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RNN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues90
DetailsTransmembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"34319232","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7RNN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsMotif: {"description":"GAS motif; ion selectivity filter","evidences":[{"source":"PubMed","id":"34319232","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7RNN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Involved in channel desensitization; the process by which the channel becomes unresponsive to proton stimulation","evidences":[{"source":"UniProtKB","id":"Q1XA76","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsSite: {"description":"Involved in the inhibition by the spider venom psalmotoxin-1","evidences":[{"source":"PubMed","id":"19654327","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsSite: {"description":"Involved in proton-dependent gating","evidences":[{"source":"PubMed","id":"19654327","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32915133","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34319232","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CFS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CFT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7RNN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsSite: {"description":"Important residue for inhibition of rat ASIC1a","evidences":[{"source":"PubMed","id":"26680001","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsSite: {"description":"Key residue for inhibition of rat ASIC1a, probably binds to rat ASIC1a F-350","evidences":[{"source":"PubMed","id":"26680001","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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