Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0007602 | biological_process | phototransduction |
A | 0009881 | molecular_function | photoreceptor activity |
A | 0016020 | cellular_component | membrane |
A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue RET A 300 |
Chain | Residue |
A | TRP96 |
A | PRO196 |
A | TRP199 |
A | ASP222 |
A | ALA225 |
A | LYS226 |
A | THR99 |
A | THR100 |
A | MET128 |
A | TRP148 |
A | SER151 |
A | THR152 |
A | TRP192 |
A | TYR195 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue R16 A 302 |
Chain | Residue |
A | THR120 |
A | GLY123 |
A | VAL223 |
A | R16305 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue R16 A 303 |
Chain | Residue |
A | SER69 |
A | ASP95 |
A | ILE156 |
A | THR193 |
A | DD9310 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue R16 A 304 |
Chain | Residue |
A | LEU133 |
A | VAL227 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue R16 A 305 |
Chain | Residue |
A | THR117 |
A | THR120 |
A | VAL124 |
A | R16302 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue D12 A 307 |
Chain | Residue |
A | ILE156 |
A | PHE161 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue R16 A 308 |
Chain | Residue |
A | SER146 |
A | PHE150 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue DD9 A 309 |
Chain | Residue |
A | GLY24 |
A | LEU28 |
A | LEU68 |
A | PHE71 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue DD9 A 310 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue DD9 A 311 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue DD9 A 312 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue R16 A 314 |
Chain | Residue |
A | SER146 |
A | LEU149 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue CA A 713 |
Chain | Residue |
A | ASP11 |
A | ASP46 |
A | ASP48 |
A | LEU240 |
A | HOH586 |
A | HOH589 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue NA A 714 |
Chain | Residue |
A | ASP11 |
A | LEU12 |
A | LEU13 |
A | ASP15 |
A | ARG17 |
A | THR20 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue CL A 715 |
Chain | Residue |
A | ALA8 |
A | GLY210 |
A | GLY212 |
A | ILE213 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue CL A 716 |
Chain | Residue |
A | LYS47 |
A | ARG115 |
A | HOH575 |
A | HOH586 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue CL A 717 |
Chain | Residue |
A | THR45 |
A | ASP46 |
A | HOH560 |
Functional Information from PROSITE/UniProt
site_id | PS00327 |
Number of Residues | 12 |
Details | BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVtAKvGF |
Chain | Residue | Details |
A | PHE218-PHE229 | |
site_id | PS00950 |
Number of Residues | 13 |
Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL |
Chain | Residue | Details |
A | ARG92-LEU104 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 38 |
Details | TOPO_DOM: Extracellular => ECO:0000250 |
Chain | Residue | Details |
A | PCA7-PRO18 | |
A | PHE72-TYR89 | |
A | SER138-ALA141 | |
A | THR203-GLY210 | |
site_id | SWS_FT_FI2 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=Helix A => ECO:0000250 |
Chain | Residue | Details |
A | GLU19-ARG40 | |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250 |
Chain | Residue | Details |
A | GLY41-ALA49 | |
A | LYS112-ASP114 | |
A | LYS171-ARG173 | |
site_id | SWS_FT_FI4 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=Helix B => ECO:0000250 |
Chain | Residue | Details |
A | ARG50-PHE71 | |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=Helix C => ECO:0000250 |
Chain | Residue | Details |
A | TYR90-ALA111 | |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=Helix D => ECO:0000250 |
Chain | Residue | Details |
A | ARG115-LEU137 | |
site_id | SWS_FT_FI7 |
Number of Residues | 28 |
Details | TRANSMEM: Helical; Name=Helix E => ECO:0000250 |
Chain | Residue | Details |
A | ILE142-ALA170 | |
site_id | SWS_FT_FI8 |
Number of Residues | 28 |
Details | TRANSMEM: Helical; Name=Helix F => ECO:0000250 |
Chain | Residue | Details |
A | GLY174-GLY202 | |
site_id | SWS_FT_FI9 |
Number of Residues | 32 |
Details | TRANSMEM: Helical; Name=Helix G => ECO:0000250 |
Chain | Residue | Details |
A | LEU211-THR243 | |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-(retinylidene)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS226 | |