6PW5
Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in Nanodiscs
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005262 | molecular_function | calcium channel activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0015279 | molecular_function | store-operated calcium channel activity |
A | 0016020 | cellular_component | membrane |
A | 0034703 | cellular_component | cation channel complex |
A | 0051480 | biological_process | regulation of cytosolic calcium ion concentration |
A | 0055085 | biological_process | transmembrane transport |
A | 0070588 | biological_process | calcium ion transmembrane transport |
A | 0070679 | molecular_function | inositol 1,4,5 trisphosphate binding |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0005262 | molecular_function | calcium channel activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0015279 | molecular_function | store-operated calcium channel activity |
B | 0016020 | cellular_component | membrane |
B | 0034703 | cellular_component | cation channel complex |
B | 0051480 | biological_process | regulation of cytosolic calcium ion concentration |
B | 0055085 | biological_process | transmembrane transport |
B | 0070588 | biological_process | calcium ion transmembrane transport |
B | 0070679 | molecular_function | inositol 1,4,5 trisphosphate binding |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0005262 | molecular_function | calcium channel activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0015279 | molecular_function | store-operated calcium channel activity |
C | 0016020 | cellular_component | membrane |
C | 0034703 | cellular_component | cation channel complex |
C | 0051480 | biological_process | regulation of cytosolic calcium ion concentration |
C | 0055085 | biological_process | transmembrane transport |
C | 0070588 | biological_process | calcium ion transmembrane transport |
C | 0070679 | molecular_function | inositol 1,4,5 trisphosphate binding |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0005262 | molecular_function | calcium channel activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0015279 | molecular_function | store-operated calcium channel activity |
D | 0016020 | cellular_component | membrane |
D | 0034703 | cellular_component | cation channel complex |
D | 0051480 | biological_process | regulation of cytosolic calcium ion concentration |
D | 0055085 | biological_process | transmembrane transport |
D | 0070588 | biological_process | calcium ion transmembrane transport |
D | 0070679 | molecular_function | inositol 1,4,5 trisphosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue PIO A 1001 |
Chain | Residue |
A | VAL437 |
A | MET755 |
A | LYS762 |
D | ARG366 |
A | THR438 |
A | TYR440 |
A | THR441 |
A | LYS442 |
A | LEU503 |
A | LEU623 |
A | SER624 |
A | SER625 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue PCW A 1002 |
Chain | Residue |
A | TYR440 |
A | TRP449 |
A | GLY450 |
A | ALA457 |
A | TRP461 |
A | ASP490 |
A | SER491 |
A | TYR500 |
A | PHE774 |
D | TYR87 |
D | TYR95 |
D | TRP125 |
D | VAL126 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue PIK A 1003 |
Chain | Residue |
A | MET564 |
A | SER565 |
A | SER566 |
A | GLY567 |
A | TRP568 |
A | MET612 |
A | LYS635 |
A | ILE639 |
A | ARG761 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PIO B 1001 |
Chain | Residue |
A | ARG366 |
B | THR438 |
B | THR441 |
B | LYS442 |
B | LEU623 |
B | SER624 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue PCW B 1002 |
Chain | Residue |
A | TYR85 |
A | TYR87 |
A | TYR95 |
A | TRP125 |
A | VAL126 |
A | TYR136 |
B | TYR440 |
B | TRP461 |
B | SER491 |
B | PRO494 |
B | TRP495 |
B | TYR500 |
B | LEU504 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue PIO C 1001 |
Chain | Residue |
B | ARG366 |
C | VAL437 |
C | THR438 |
C | TYR440 |
C | THR441 |
C | LYS442 |
C | LEU503 |
C | LEU623 |
C | SER624 |
C | SER625 |
C | MET755 |
C | LYS762 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue PIK C 1003 |
Chain | Residue |
C | MET564 |
C | SER565 |
C | SER566 |
C | GLY567 |
C | MET612 |
C | LYS635 |
C | ILE639 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PIO D 1001 |
Chain | Residue |
C | ARG366 |
D | THR438 |
D | THR441 |
D | LYS442 |
D | LEU623 |
D | SER624 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue PCW D 1002 |
Chain | Residue |
C | TYR87 |
C | TYR95 |
C | TRP125 |
C | VAL126 |
C | TYR136 |
D | TYR440 |
D | TRP461 |
D | SER491 |
D | PRO494 |
D | TRP495 |
D | TYR500 |
D | LEU504 |
site_id | AD1 |
Number of Residues | 18 |
Details | binding site for residue PIK B 1003 |
Chain | Residue |
B | ASN603 |
B | LEU605 |
B | LEU606 |
B | ALA607 |
B | ALA608 |
B | MET612 |
B | PHE615 |
B | LYS635 |
B | ILE639 |
A | PHE727 |
B | MET564 |
B | SER565 |
B | GLY567 |
B | VAL570 |
B | MET571 |
B | LEU600 |
B | VAL601 |
B | VAL602 |
site_id | AD2 |
Number of Residues | 16 |
Details | binding site for residue PCW C 1002 |
Chain | Residue |
B | TYR87 |
B | TYR95 |
B | TRP125 |
B | VAL126 |
C | MET435 |
C | TYR440 |
C | TRP449 |
C | GLY450 |
C | ALA457 |
C | TRP461 |
C | ASP490 |
C | ARG492 |
C | PHE493 |
C | PRO494 |
C | TYR500 |
C | PHE774 |
site_id | AD3 |
Number of Residues | 18 |
Details | binding site for residue PIK D 1003 |
Chain | Residue |
C | PHE727 |
D | MET564 |
D | SER565 |
D | GLY567 |
D | VAL570 |
D | MET571 |
D | LEU600 |
D | VAL601 |
D | VAL602 |
D | ASN603 |
D | LEU605 |
D | LEU606 |
D | ALA607 |
D | ALA608 |
D | MET612 |
D | PHE615 |
D | LYS635 |
D | ILE639 |