7MZ7
Cryo-EM structure of minimal TRPV1 with 4 partially bound RTX
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 |