5E1J
Structure of voltage-gated two-pore channel TPC1 from Arabidopsis thaliana
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000325 | cellular_component | plant-type vacuole |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005245 | molecular_function | voltage-gated calcium channel activity |
A | 0005262 | molecular_function | calcium channel activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005773 | cellular_component | vacuole |
A | 0005774 | cellular_component | vacuolar membrane |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006816 | biological_process | calcium ion transport |
A | 0009845 | biological_process | seed germination |
A | 0010119 | biological_process | regulation of stomatal movement |
A | 0016020 | cellular_component | membrane |
A | 0019722 | biological_process | calcium-mediated signaling |
A | 0034702 | cellular_component | monoatomic ion channel complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0055085 | biological_process | transmembrane transport |
A | 0070588 | biological_process | calcium ion transmembrane transport |
A | 0080141 | biological_process | regulation of jasmonic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue BA A 801 |
Chain | Residue |
A | GLU605 |
A | GLU605 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue BA A 803 |
Chain | Residue |
A | HOH904 |
A | HOH901 |
A | HOH901 |
A | HOH902 |
A | HOH902 |
A | HOH903 |
A | HOH903 |
A | HOH904 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue BA A 804 |
Chain | Residue |
A | GLU239 |
A | ASP240 |
A | GLU457 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue BA A 805 |
Chain | Residue |
A | ASP240 |
A | ASP454 |
A | GLU528 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue BA A 806 |
Chain | Residue |
A | ASN339 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CA A 809 |
Chain | Residue |
A | ASP335 |
A | ASP337 |
A | ASN339 |
A | GLU341 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CA A 810 |
Chain | Residue |
A | SER120 |
A | GLU124 |
A | ASP170 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 309 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-ASP71 | |
A | GLU142-ALA158 | |
A | ARG200-ASN218 | |
A | VAL304-ARG428 | |
A | GLY487-ARG498 | |
A | ASN547-THR557 | |
A | GLU673-THR733 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S1 of repeat I => ECO:0000255 |
Chain | Residue | Details |
A | LEU72-TRP92 |
site_id | SWS_FT_FI3 |
Number of Residues | 133 |
Details | TOPO_DOM: Vacuolar => ECO:0000255 |
Chain | Residue | Details |
A | CYS93-SER120 | |
A | ASP180 | |
A | ASP240-LEU245 | |
A | LEU261-SER282 | |
A | GLU450-GLN465 | |
A | GLU520-GLU528 | |
A | TYR579-ASP615 | |
A | ASN631-TYR651 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat I => ECO:0000255 |
Chain | Residue | Details |
A | ILE121-TYR141 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S3 of repeat I => ECO:0000255 |
Chain | Residue | Details |
A | CYS159-PHE179 |
site_id | SWS_FT_FI6 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Voltage-sensor; Name=S4 of repeat I => ECO:0000255 |
Chain | Residue | Details |
A | PHE181-ILE199 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S5 of repeat I => ECO:0000255 |
Chain | Residue | Details |
A | ILE219-GLU239 |
site_id | SWS_FT_FI8 |
Number of Residues | 14 |
Details | INTRAMEM: Pore-forming; Name=Pore-forming 1 |
Chain | Residue | Details |
A | THR246-ILE260 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000255 |
Chain | Residue | Details |
A | VAL283-VAL303 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S1 of repeat II => ECO:0000255 |
Chain | Residue | Details |
A | SER429-VAL449 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat II => ECO:0000255 |
Chain | Residue | Details |
A | VAL466-TYR486 |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S3 of repeat II => ECO:0000255 |
Chain | Residue | Details |
A | PHE499-ASP519 |
site_id | SWS_FT_FI13 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Voltage-sensor; Name=S4 of repeat II => ECO:0000255 |
Chain | Residue | Details |
A | TRP529-MET546 |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S5 of repeat II => ECO:0000255 |
Chain | Residue | Details |
A | PHE558-ILE578 |
site_id | SWS_FT_FI15 |
Number of Residues | 14 |
Details | INTRAMEM: Pore-forming; Name=Pore-forming 2 |
Chain | Residue | Details |
A | TYR616-GLY630 |
site_id | SWS_FT_FI16 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat II => ECO:0000255 |
Chain | Residue | Details |
A | PHE652-LEU672 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | MET1 |