9C2C
Cryo-EM structure of the human P2X1 receptor in the NF449-bound inhibited state
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS01212 |
| Number of Residues | 27 |
| Details | P2X_RECEPTOR ATP P2X receptors signature. GGvVGItIdWhCDLDwhvrhCrPiYeF |
| Chain | Residue | Details |
| A | GLY250-PHE276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 201 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P56373 |
| Chain | Residue | Details |
| A | MET1-LYS28 | |
| A | LYS359-SER399 | |
| C | MET1-LYS28 | |
| C | LYS359-SER399 | |
| B | MET1-LYS28 | |
| B | LYS359-SER399 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 63 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL29-LEU50 | |
| C | VAL29-LEU50 | |
| B | VAL29-LEU50 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 861 |
| Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P56373 |
| Chain | Residue | Details |
| A | TYR51-GLY338 | |
| C | TYR51-GLY338 | |
| B | TYR51-GLY338 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 57 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
| Chain | Residue | Details |
| A | ILE339-PRO358 | |
| C | ILE339-PRO358 | |
| B | ILE339-PRO358 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:F8W463 |
| Chain | Residue | Details |
| A | LYS68 | |
| C | LYS140 | |
| C | THR186 | |
| C | ASN290 | |
| C | ARG292 | |
| C | LYS309 | |
| B | LYS68 | |
| B | LYS70 | |
| B | LYS140 | |
| B | THR186 | |
| B | ASN290 | |
| A | LYS70 | |
| B | ARG292 | |
| B | LYS309 | |
| A | LYS140 | |
| A | THR186 | |
| A | ASN290 | |
| A | ARG292 | |
| A | LYS309 | |
| C | LYS68 | |
| C | LYS70 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P56373 |
| Chain | Residue | Details |
| A | SER286 | |
| C | SER286 | |
| B | SER286 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:22971236 |
| Chain | Residue | Details |
| A | SER387 | |
| A | SER388 | |
| C | SER387 | |
| C | SER388 | |
| B | SER387 | |
| B | SER388 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:22971236 |
| Chain | Residue | Details |
| A | THR389 | |
| C | THR389 | |
| B | THR389 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN153 | |
| B | ASN184 | |
| B | ASN242 | |
| B | ASN300 | |
| A | ASN184 | |
| A | ASN242 | |
| A | ASN300 | |
| C | ASN153 | |
| C | ASN184 | |
| C | ASN242 | |
| C | ASN300 | |
| B | ASN153 |
