Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9LX5

Cryo-EM structure of the P2X1 receptor bound to ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001614molecular_functionpurinergic nucleotide receptor activity
A0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
A0005216molecular_functionmonoatomic ion channel activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0033198biological_processresponse to ATP
A0098655biological_processmonoatomic cation transmembrane transport
B0001614molecular_functionpurinergic nucleotide receptor activity
B0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
B0005216molecular_functionmonoatomic ion channel activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0033198biological_processresponse to ATP
B0098655biological_processmonoatomic cation transmembrane transport
C0001614molecular_functionpurinergic nucleotide receptor activity
C0004931molecular_functionextracellularly ATP-gated monoatomic cation channel activity
C0005216molecular_functionmonoatomic ion channel activity
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0033198biological_processresponse to ATP
C0098655biological_processmonoatomic cation transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS01212
Number of Residues27
DetailsP2X_RECEPTOR ATP P2X receptors signature. GGvVGItIdWhCDLDwhvrhCrPiYeF
ChainResidueDetails
AGLY250-PHE276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues861
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"P56373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsRegion: {"description":"Pore-forming motif","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"F8W463","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P56373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon