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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8JV6

Cryo-EM structure of the zebrafish P2X4 receptor in complex with BAY-1797

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001614molecular_functionpurinergic nucleotide receptor activity
A0002135molecular_functionCTP binding
A0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
A0005216molecular_functionmonoatomic ion channel activity
A0005524molecular_functionATP binding
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0006816biological_processcalcium ion transport
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
A0017076molecular_functionpurine nucleotide binding
A0033198biological_processresponse to ATP
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035381molecular_functionATP-gated ion channel activity
A0035590biological_processpurinergic nucleotide receptor signaling pathway
A0042802molecular_functionidentical protein binding
A0060079biological_processexcitatory postsynaptic potential
A0098655biological_processmonoatomic cation transmembrane transport
A0098794cellular_componentpostsynapse
A1902495cellular_componenttransmembrane transporter complex
B0000166molecular_functionnucleotide binding
B0001614molecular_functionpurinergic nucleotide receptor activity
B0002135molecular_functionCTP binding
B0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
B0005216molecular_functionmonoatomic ion channel activity
B0005524molecular_functionATP binding
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006812biological_processmonoatomic cation transport
B0006816biological_processcalcium ion transport
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
B0017076molecular_functionpurine nucleotide binding
B0033198biological_processresponse to ATP
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0035381molecular_functionATP-gated ion channel activity
B0035590biological_processpurinergic nucleotide receptor signaling pathway
B0042802molecular_functionidentical protein binding
B0060079biological_processexcitatory postsynaptic potential
B0098655biological_processmonoatomic cation transmembrane transport
B0098794cellular_componentpostsynapse
B1902495cellular_componenttransmembrane transporter complex
C0000166molecular_functionnucleotide binding
C0001614molecular_functionpurinergic nucleotide receptor activity
C0002135molecular_functionCTP binding
C0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
C0005216molecular_functionmonoatomic ion channel activity
C0005524molecular_functionATP binding
C0005765cellular_componentlysosomal membrane
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006812biological_processmonoatomic cation transport
C0006816biological_processcalcium ion transport
C0015276molecular_functionligand-gated monoatomic ion channel activity
C0016020cellular_componentmembrane
C0017076molecular_functionpurine nucleotide binding
C0033198biological_processresponse to ATP
C0034220biological_processmonoatomic ion transmembrane transport
C0034702cellular_componentmonoatomic ion channel complex
C0035381molecular_functionATP-gated ion channel activity
C0035590biological_processpurinergic nucleotide receptor signaling pathway
C0042802molecular_functionidentical protein binding
C0060079biological_processexcitatory postsynaptic potential
C0098655biological_processmonoatomic cation transmembrane transport
C0098794cellular_componentpostsynapse
C1902495cellular_componenttransmembrane transporter complex
Functional Information from PROSITE/UniProt
site_idPS01212
Number of Residues27
DetailsP2X_RECEPTOR ATP P2X receptors signature. GGvMGVqIrWdCDLDmpqswCvPrYtF
ChainResidueDetails
AGLY253-PHE279
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues855
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"28332633","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5WZY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28332633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WZY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22535247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DW1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19641588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3I5D","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19641588","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22535247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H9V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3I5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DW0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DW1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WZY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19641588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3I5D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19641588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3I5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DW0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DW1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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