9C48
Cryo-EM structure of the full-length human P2X4 receptor in the ATP-bound desensitized state
Functional Information from PROSITE/UniProt
site_id | PS01212 |
Number of Residues | 27 |
Details | P2X_RECEPTOR ATP P2X receptors signature. GGiMGIqVnWdCNLDraaslClPrYsF |
Chain | Residue | Details |
A | GLY250-PHE276 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 180 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-ARG33 | |
A | CYS360-GLN388 | |
B | MET1-ARG33 | |
B | CYS360-GLN388 | |
C | MET1-ARG33 | |
C | CYS360-GLN388 |
site_id | SWS_FT_FI2 |
Number of Residues | 60 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | ALA34-TYR54 | |
B | ALA34-TYR54 | |
C | ALA34-TYR54 |
site_id | SWS_FT_FI3 |
Number of Residues | 849 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | GLN55-ASN338 | |
B | GLN55-ASN338 | |
C | GLN55-ASN338 |
site_id | SWS_FT_FI4 |
Number of Residues | 60 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | ILE339-TYR359 | |
B | ILE339-TYR359 | |
C | ILE339-TYR359 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:F8W463 |
Chain | Residue | Details |
A | LYS67 | |
B | THR186 | |
B | LEU188 | |
B | ASN293 | |
B | ARG295 | |
B | LYS313 | |
C | LYS67 | |
C | LYS69 | |
C | THR186 | |
C | LEU188 | |
C | ASN293 | |
A | LYS69 | |
C | ARG295 | |
C | LYS313 | |
A | THR186 | |
A | LEU188 | |
A | ASN293 | |
A | ARG295 | |
A | LYS313 | |
B | LYS67 | |
B | LYS69 |
site_id | SWS_FT_FI6 |
Number of Residues | 15 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN75 | |
B | ASN208 | |
C | ASN75 | |
C | ASN110 | |
C | ASN153 | |
C | ASN199 | |
C | ASN208 | |
A | ASN110 | |
A | ASN153 | |
A | ASN199 | |
A | ASN208 | |
B | ASN75 | |
B | ASN110 | |
B | ASN153 | |
B | ASN199 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN184 | |
B | ASN184 | |
C | ASN184 |