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3H9V

Crystal structure of the ATP-gated P2X4 ion channel in the closed, apo state at 3.1 Angstroms

Functional Information from GO Data
ChainGOidnamespacecontents
A0001614molecular_functionpurinergic nucleotide receptor activity
A0002135molecular_functionCTP binding
A0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
A0005216molecular_functionmonoatomic ion channel activity
A0005524molecular_functionATP binding
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0006816biological_processcalcium ion transport
A0007165biological_processsignal transduction
A0015267molecular_functionchannel activity
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
A0060079biological_processexcitatory postsynaptic potential
A0070588biological_processcalcium ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
A0098794cellular_componentpostsynapse
A1902495cellular_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 Residues40
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:28332633, ECO:0007744|PDB:5WZY
ChainResidueDetails
APHE37-TYR57
AALA344-MET364

site_idSWS_FT_FI2
Number of Residues285
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:28332633, ECO:0007744|PDB:5WZY
ChainResidueDetails
AGLN58-GLY343

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:28332633, ECO:0007744|PDB:5WZY
ChainResidueDetails
ALYS70
ALYS72
AARG143
ATHR189
AASN296
AARG298
ALYS316

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22535247, ECO:0007744|PDB:4DW1
ChainResidueDetails
ALEU191

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19641588, ECO:0000312|PDB:3I5D
ChainResidueDetails
ALYS78

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19641588, ECO:0000269|PubMed:22535247, ECO:0007744|PDB:3H9V, ECO:0007744|PDB:3I5D, ECO:0007744|PDB:4DW0, ECO:0007744|PDB:4DW1, ECO:0007744|PDB:5WZY
ChainResidueDetails
AASN113

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19641588, ECO:0007744|PDB:3I5D
ChainResidueDetails
AARG187

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19641588, ECO:0007744|PDB:3I5D, ECO:0007744|PDB:4DW0, ECO:0007744|PDB:4DW1
ChainResidueDetails
AASN213

224201

PDB entries from 2024-08-28

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