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4NTW

Structure of acid-sensing ion channel in complex with snake toxin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005272molecular_functionsodium channel activity
A0006814biological_processsodium ion transport
A0015280molecular_functionligand-gated sodium channel activity
A0016020cellular_componentmembrane
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0030414molecular_functionpeptidase inhibitor activity
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
B0099106molecular_functionion channel regulator activity
C0004623molecular_functionphospholipase A2 activity
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0035821biological_processmodulation of process of another organism
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonate secretion
C0090729molecular_functiontoxin activity
C0099106molecular_functionion channel regulator activity
Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. CYEDPPF
ChainResidueDetails
BCYS7-PHE13

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCNCDRTAtLC
ChainResidueDetails
CVAL90-CYS100

site_idPS01206
Number of Residues21
DetailsASC Amiloride-sensitive sodium channels signature. YsiTaCridCeTryLVenCnC
ChainResidueDetails
ATYR304-CYS324

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24507937","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NTW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues29
DetailsTransmembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"24507937","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NTW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsMotif: {"description":"GAS motif; ion selectivity filter","evidences":[{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24507937","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Involved in channel desensitization; the process by which the channel becomes unresponsive to proton stimulation","evidences":[{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Involved in proton-dependent gating","evidences":[{"source":"UniProtKB","id":"P78348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17882215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22760635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QTS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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