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9C48

Cryo-EM structure of the full-length human P2X4 receptor in the ATP-bound desensitized state

Functional Information from PROSITE/UniProt
site_idPS01212
Number of Residues27
DetailsP2X_RECEPTOR ATP P2X receptors signature. GGiMGIqVnWdCNLDraaslClPrYsF
ChainResidueDetails
AGLY250-PHE276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues180
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ARG33
ACYS360-GLN388
BMET1-ARG33
BCYS360-GLN388
CMET1-ARG33
CCYS360-GLN388

site_idSWS_FT_FI2
Number of Residues60
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AALA34-TYR54
BALA34-TYR54
CALA34-TYR54

site_idSWS_FT_FI3
Number of Residues849
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AGLN55-ASN338
BGLN55-ASN338
CGLN55-ASN338

site_idSWS_FT_FI4
Number of Residues60
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AILE339-TYR359
BILE339-TYR359
CILE339-TYR359

site_idSWS_FT_FI5
Number of Residues21
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:F8W463
ChainResidueDetails
ALYS67
BTHR186
BLEU188
BASN293
BARG295
BLYS313
CLYS67
CLYS69
CTHR186
CLEU188
CASN293
ALYS69
CARG295
CLYS313
ATHR186
ALEU188
AASN293
AARG295
ALYS313
BLYS67
BLYS69

site_idSWS_FT_FI6
Number of Residues15
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN75
BASN208
CASN75
CASN110
CASN153
CASN199
CASN208
AASN110
AASN153
AASN199
AASN208
BASN75
BASN110
BASN153
BASN199

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN184
BASN184
CASN184

232829

PDB entries from 2025-03-12

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