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 |
| B | 0005216 | molecular_function | monoatomic ion channel activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0007602 | biological_process | phototransduction |
| B | 0009881 | molecular_function | photoreceptor activity |
| B | 0016020 | cellular_component | membrane |
| B | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RET A 255 |
| Chain | Residue |
| A | TRP92 |
| A | ASP218 |
| A | ALA221 |
| A | LYS222 |
| A | THR96 |
| A | TRP144 |
| A | SER147 |
| A | THR148 |
| A | TRP188 |
| A | TYR191 |
| A | PRO192 |
| A | TRP195 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RET B 255 |
| Chain | Residue |
| B | TRP92 |
| B | THR96 |
| B | MET124 |
| B | TRP144 |
| B | SER147 |
| B | THR148 |
| B | MET151 |
| B | TRP188 |
| B | TYR191 |
| B | PRO192 |
| B | TRP195 |
| B | ASP218 |
| B | LYS222 |
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 | PHE214-PHE225 | |
| site_id | PS00950 |
| Number of Residues | 13 |
| Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL |
| Chain | Residue | Details |
| A | ARG88-LEU100 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix C","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=Helix D","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 56 |
| Details | Transmembrane: {"description":"Helical; Name=Helix E","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 54 |
| Details | Transmembrane: {"description":"Helical; Name=Helix F","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(retinylidene)lysine"} |
