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9LX5

Cryo-EM structure of the P2X1 receptor bound to ATP

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

245011

PDB entries from 2025-11-19

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