5IRX
Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc
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 |
E | 0005515 | molecular_function | protein binding |
E | 0005576 | cellular_component | extracellular region |
E | 0008289 | molecular_function | lipid binding |
E | 0035821 | biological_process | modulation of process of another organism |
E | 0090729 | molecular_function | toxin activity |
E | 0099106 | molecular_function | ion channel regulator activity |
F | 0005515 | molecular_function | protein binding |
F | 0005576 | cellular_component | extracellular region |
F | 0008289 | molecular_function | lipid binding |
F | 0035821 | biological_process | modulation of process of another organism |
F | 0090729 | molecular_function | toxin activity |
F | 0099106 | molecular_function | ion channel regulator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue 6O8 A 801 |
Chain | Residue |
A | ASN437 |
A | VAL440 |
A | TYR487 |
A | PHE488 |
A | ARG491 |
A | GLU513 |
A | PHE516 |
A | TYR554 |
A | TYR555 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue 6OE A 802 |
Chain | Residue |
A | SER629 |
A | TYR631 |
C | TYR453 |
F | ALA66 |
F | PHE67 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue 6OE A 803 |
Chain | Residue |
A | SER532 |
A | ARG534 |
F | 6O9102 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue 6EU A 804 |
Chain | Residue |
A | TYR511 |
A | SER512 |
A | ILE514 |
A | LEU515 |
A | ALA546 |
A | MET547 |
A | THR550 |
A | ASN551 |
A | LEU553 |
A | TYR554 |
A | ARG557 |
A | ALA566 |
A | ILE569 |
A | ILE573 |
B | PHE591 |
B | ILE668 |
B | LEU669 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue 6O8 B 801 |
Chain | Residue |
B | ASN437 |
B | VAL440 |
B | TYR487 |
B | PHE488 |
B | ARG491 |
B | GLU513 |
B | PHE516 |
B | TYR554 |
B | TYR555 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue 6OE B 802 |
Chain | Residue |
B | SER532 |
B | ARG534 |
F | 6O9101 |
site_id | AC7 |
Number of Residues | 17 |
Details | binding site for residue 6EU B 803 |
Chain | Residue |
B | TYR511 |
B | SER512 |
B | ILE514 |
B | LEU515 |
B | ALA546 |
B | MET547 |
B | THR550 |
B | ASN551 |
B | LEU553 |
B | TYR554 |
B | ARG557 |
B | ALA566 |
B | ILE569 |
B | ILE573 |
D | PHE591 |
D | ILE668 |
D | LEU669 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue 6O8 C 801 |
Chain | Residue |
C | ASN437 |
C | VAL440 |
C | TYR487 |
C | PHE488 |
C | ARG491 |
C | GLU513 |
C | PHE516 |
C | TYR554 |
C | TYR555 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue 6OE C 802 |
Chain | Residue |
C | ARG534 |
E | 6O9101 |
site_id | AD1 |
Number of Residues | 17 |
Details | binding site for residue 6EU C 803 |
Chain | Residue |
A | PHE591 |
A | ILE668 |
A | LEU669 |
C | TYR511 |
C | SER512 |
C | ILE514 |
C | LEU515 |
C | ALA546 |
C | MET547 |
C | THR550 |
C | ASN551 |
C | LEU553 |
C | TYR554 |
C | ARG557 |
C | ALA566 |
C | ILE569 |
C | ILE573 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue 6O8 D 801 |
Chain | Residue |
D | TYR555 |
D | ASN437 |
D | VAL440 |
D | TYR487 |
D | PHE488 |
D | ARG491 |
D | GLU513 |
D | PHE516 |
D | TYR554 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue 6O9 D 802 |
Chain | Residue |
D | ARG534 |
D | 6OE804 |
E | VAL50 |
E | TRP53 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue 6OE D 803 |
Chain | Residue |
B | TYR453 |
D | SER629 |
D | TYR631 |
E | ALA66 |
E | PHE67 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue 6OE D 804 |
Chain | Residue |
D | SER532 |
D | ARG534 |
D | 6O9802 |
site_id | AD6 |
Number of Residues | 17 |
Details | binding site for residue 6EU D 805 |
Chain | Residue |
C | PHE591 |
C | ILE668 |
C | LEU669 |
D | TYR511 |
D | SER512 |
D | ILE514 |
D | LEU515 |
D | ALA546 |
D | MET547 |
D | THR550 |
D | ASN551 |
D | LEU553 |
D | TYR554 |
D | ARG557 |
D | ALA566 |
D | ILE569 |
D | ILE573 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue 6O9 E 101 |
Chain | Residue |
C | ARG534 |
C | 6OE802 |
E | GLU7 |
E | VAL8 |
E | TRP11 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue 6OE E 102 |
Chain | Residue |
C | SER629 |
C | TYR631 |
D | TYR453 |
E | GLU26 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue 6O9 F 101 |
Chain | Residue |
B | ARG534 |
B | 6OE802 |
F | GLU7 |
F | VAL8 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue 6O9 F 102 |
Chain | Residue |
A | ARG534 |
A | 6OE803 |
F | GLU49 |
F | VAL50 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue 6OE F 103 |
Chain | Residue |
A | TYR453 |
B | SER629 |
B | TYR631 |
F | GLU26 |
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 | |
A | TYR472-LEU497 | |
A | TYR511-PHE531 | |
A | GLU536-THR556 | |
A | MET572-ILE599 | |
A | VAL658-VAL686 | |
B | ILE433-TYR453 | |
B | TYR472-LEU497 | |
B | TYR511-PHE531 | |
B | GLU536-THR556 | |
B | MET572-ILE599 | |
B | VAL658-VAL686 | |
C | ILE433-TYR453 | |
C | TYR472-LEU497 | |
C | TYR511-PHE531 | |
C | GLU536-THR556 | |
C | MET572-ILE599 | |
C | VAL658-VAL686 | |
D | ILE433-TYR453 | |
D | TYR472-LEU497 | |
D | TYR511-PHE531 | |
D | MET572-ILE599 | |
D | VAL658-VAL686 | |
D | GLU536-THR556 |
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 | |
A | SER532-LYS535 | |
A | GLU600-PHE649 | |
B | TYR454-ASP471 | |
B | SER532-LYS535 | |
B | GLU600-PHE649 | |
C | TYR454-ASP471 | |
C | SER532-LYS535 | |
C | GLU600-PHE649 | |
D | TYR454-ASP471 | |
D | SER532-LYS535 | |
D | 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 | |
B | GLN498-SER510 | |
B | ARG557-LYS571 | |
C | GLN498-SER510 | |
C | ARG557-LYS571 | |
D | GLN498-SER510 | |
D | 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 | TYR627-PHE649 | |
B | TYR627-PHE649 | |
C | TYR627-PHE649 | |
D | TYR627-PHE649 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0007744|PDB:2PNN |
Chain | Residue | Details |
B | LYS155 | |
B | GLU210 | |
C | ARG115 | |
C | LYS155 | |
C | GLU210 | |
D | ARG115 | |
D | LYS155 | |
D | GLU210 | |
A | ARG115 | |
A | LYS155 | |
A | GLU210 | |
B | ARG115 |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN |
Chain | Residue | Details |
B | ASN164 | |
B | TYR199 | |
C | LYS160 | |
C | ASN164 | |
C | TYR199 | |
D | LYS160 | |
D | ASN164 | |
D | TYR199 | |
A | LYS160 | |
A | ASN164 | |
A | TYR199 | |
B | LYS160 |
site_id | SWS_FT_FI7 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX |
Chain | Residue | Details |
B | THR550 | |
B | ARG557 | |
C | TYR511 | |
C | THR550 | |
C | ARG557 | |
D | TYR511 | |
D | THR550 | |
D | ARG557 | |
A | TYR511 | |
A | THR550 | |
A | ARG557 | |
B | TYR511 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9R186 |
Chain | Residue | Details |
A | ASP646 | |
B | ASP646 | |
C | ASP646 | |
D | ASP646 |
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 | |
B | SER116 | |
C | SER116 | |
D | 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 | |
B | THR144 | |
B | THR370 | |
C | THR144 | |
C | THR370 | |
D | THR144 | |
D | 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 | |
B | SER502 | |
C | SER502 | |
D | SER502 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:14630912 |
Chain | Residue | Details |
A | THR704 | |
B | THR704 | |
C | THR704 | |
D | THR704 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 |
Chain | Residue | Details |
A | TYR627 | |
B | TYR627 | |
C | TYR627 | |
D | TYR627 |