7MZE
Cryo-EM structure of minimal TRPV1 with 2 bound RTX in opposite pockets
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0005216 | molecular_function | monoatomic ion channel activity |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0016020 | cellular_component | membrane |
| B | 0055085 | biological_process | transmembrane transport |
| C | 0005216 | molecular_function | monoatomic ion channel activity |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0016020 | cellular_component | membrane |
| C | 0055085 | biological_process | transmembrane transport |
| D | 0005216 | molecular_function | monoatomic ion channel activity |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0016020 | cellular_component | membrane |
| D | 0055085 | biological_process | transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 560 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 |
| Chain | Residue | Details |
| A | ILE433-TYR453 | |
| D | GLU536-THR556 | |
| D | MET572-ILE599 | |
| D | LEU681-GLU709 | |
| B | ILE433-TYR453 | |
| B | TYR472-LEU497 | |
| B | TYR511-PHE531 | |
| B | GLU536-THR556 | |
| B | MET572-ILE599 | |
| B | LEU681-GLU709 | |
| C | ILE433-TYR453 | |
| A | TYR472-LEU497 | |
| C | TYR472-LEU497 | |
| C | TYR511-PHE531 | |
| C | GLU536-THR556 | |
| C | MET572-ILE599 | |
| C | LEU681-GLU709 | |
| A | TYR511-PHE531 | |
| A | GLU536-THR556 | |
| A | MET572-ILE599 | |
| A | LEU681-GLU709 | |
| D | ILE433-TYR453 | |
| D | TYR472-LEU497 | |
| D | TYR511-PHE531 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 184 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 |
| Chain | Residue | Details |
| A | TYR454-ASP471 | |
| C | TYR454-ASP471 | |
| C | SER532-LYS535 | |
| C | GLU600-PHE649 | |
| A | SER532-LYS535 | |
| A | GLU600-PHE649 | |
| D | TYR454-ASP471 | |
| D | SER532-LYS535 | |
| D | GLU600-PHE649 | |
| B | TYR454-ASP471 | |
| B | SER532-LYS535 | |
| B | GLU600-PHE649 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 104 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 |
| Chain | Residue | Details |
| A | GLN498-SER510 | |
| A | ARG557-LYS571 | |
| D | GLN498-SER510 | |
| D | ARG557-LYS571 | |
| B | GLN498-SER510 | |
| B | ARG557-LYS571 | |
| C | GLN498-SER510 | |
| C | ARG557-LYS571 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 88 |
| Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 |
| Chain | Residue | Details |
| A | THR650-ILE672 | |
| D | THR650-ILE672 | |
| B | THR650-ILE672 | |
| C | THR650-ILE672 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2PNN |
| Chain | Residue | Details |
| A | ARG115 | |
| C | ARG115 | |
| C | LYS155 | |
| C | GLU210 | |
| A | LYS155 | |
| A | GLU210 | |
| D | ARG115 | |
| D | LYS155 | |
| D | GLU210 | |
| B | ARG115 | |
| B | LYS155 | |
| B | GLU210 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN |
| Chain | Residue | Details |
| A | LYS160 | |
| C | LYS160 | |
| C | ASN164 | |
| C | TYR199 | |
| A | ASN164 | |
| A | TYR199 | |
| D | LYS160 | |
| D | ASN164 | |
| D | TYR199 | |
| B | LYS160 | |
| B | ASN164 | |
| B | TYR199 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX |
| Chain | Residue | Details |
| A | TYR511 | |
| C | TYR511 | |
| C | THR550 | |
| C | ARG557 | |
| A | THR550 | |
| A | ARG557 | |
| D | TYR511 | |
| D | THR550 | |
| D | ARG557 | |
| B | TYR511 | |
| B | THR550 | |
| B | ARG557 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9R186 |
| Chain | Residue | Details |
| A | LEU669 | |
| D | LEU669 | |
| B | LEU669 | |
| C | LEU669 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852 |
| Chain | Residue | Details |
| A | SER116 | |
| D | SER116 | |
| B | SER116 | |
| C | SER116 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 |
| Chain | Residue | Details |
| A | THR144 | |
| A | THR370 | |
| D | THR144 | |
| D | THR370 | |
| B | THR144 | |
| B | THR370 | |
| C | THR144 | |
| C | THR370 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912 |
| Chain | Residue | Details |
| A | SER502 | |
| D | SER502 | |
| B | SER502 | |
| C | SER502 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:14630912 |
| Chain | Residue | Details |
| A | GLN727 | |
| D | GLN727 | |
| B | GLN727 | |
| C | GLN727 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 |
| Chain | Residue | Details |
| A | TYR627 | |
| D | TYR627 | |
| B | TYR627 | |
| C | TYR627 |
