5DQQ
Structure, inhibition and regulation of 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 | 0034220 | biological_process | monoatomic ion transmembrane transport |
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 | 1 |
Details | binding site for residue CA A 802 |
Chain | Residue |
A | GLU374 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue CA A 803 |
Chain | Residue |
A | ASN612 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CA A 804 |
Chain | Residue |
A | GLU239 |
A | HOH943 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CA A 805 |
Chain | Residue |
A | ASP240 |
A | ASP454 |
A | GLU528 |
A | HOH932 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA A 806 |
Chain | Residue |
A | ASP337 |
A | ASN339 |
A | GLU341 |
A | ASP343 |
A | GLN346 |
A | ASP335 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CA A 807 |
Chain | Residue |
A | TRP92 |
A | GLU124 |
A | ASP170 |
A | HOH918 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue PLM A 808 |
Chain | Residue |
A | MET237 |
A | SER277 |
A | VAL283 |
A | LEU533 |
A | HOH906 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue 66R A 809 |
Chain | Residue |
A | TRP232 |
A | TYR251 |
A | PHE444 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S1 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 88 |
Details | Topological domain: {"description":"Vacuolar","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S2 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 55 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S5 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 14 |
Details | Intramembrane: {"description":"Pore-forming; Name=Pore-forming 1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S6 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S2 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 17 |
Details | Transmembrane: {"description":"Helical; Voltage-sensor; Name=S4 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 14 |
Details | Intramembrane: {"description":"Pore-forming; Name=Pore-forming 2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 35 |
Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 35 |
Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 9 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |