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 | 0034220 | biological_process | monoatomic ion 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 | 0034220 | biological_process | monoatomic ion transmembrane transport |
| D | 0005216 | molecular_function | monoatomic ion channel activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0007602 | biological_process | phototransduction |
| D | 0009881 | molecular_function | photoreceptor activity |
| D | 0016020 | cellular_component | membrane |
| D | 0034220 | biological_process | monoatomic ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RET A 292 |
| Chain | Residue |
| A | TRP127 |
| A | THR131 |
| A | GLY163 |
| A | TYR180 |
| A | SER183 |
| A | TRP222 |
| A | TYR225 |
| A | ASP252 |
| A | LYS256 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 22B A 300 |
| Chain | Residue |
| A | ILE49 |
| A | THR56 |
| A | LYS65 |
| A | ILE72 |
| D | THR151 |
| D | PHE155 |
| D | ALA185 |
| D | VAL189 |
| D | ILE193 |
| D | GLU197 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR A 401 |
| Chain | Residue |
| A | THR126 |
| A | SER130 |
| A | LYS256 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 402 |
| Chain | Residue |
| A | ASN145 |
| B | LYS65 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 293 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RET B 292 |
| Chain | Residue |
| B | TRP127 |
| B | THR131 |
| B | TYR180 |
| B | SER183 |
| B | TRP222 |
| B | TYR225 |
| B | PRO226 |
| B | LYS256 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 22B B 300 |
| Chain | Residue |
| A | PHE155 |
| A | VAL189 |
| A | ILE193 |
| A | GLU197 |
| B | ILE49 |
| B | VAL53 |
| B | THR56 |
| B | LYS65 |
| B | ILE72 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 401 |
| Chain | Residue |
| B | THR126 |
| B | SER130 |
| B | LYS256 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE RET D 292 |
| Chain | Residue |
| D | TRP127 |
| D | MET159 |
| D | TYR180 |
| D | SER183 |
| D | TRP222 |
| D | TYR225 |
| D | PRO226 |
| D | TRP229 |
| D | ASP252 |
| D | LYS256 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR D 402 |
| Chain | Residue |
| B | ASN145 |
| D | LYS65 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR D 401 |
| Chain | Residue |
| D | THR126 |
| D | SER130 |
| D | LYS256 |
Functional Information from PROSITE/UniProt
| site_id | PS00950 |
| Number of Residues | 13 |
| Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYlTWaLSTPMIL |
| Chain | Residue | Details |
| A | ARG123-LEU135 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 75 |
| Details | Transmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 69 |
| Details | Transmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 129 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 63 |
| Details | Transmembrane: {"description":"Helical; Name=Helix C","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 69 |
| Details | Transmembrane: {"description":"Helical; Name=Helix D","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 66 |
| Details | Transmembrane: {"description":"Helical; Name=Helix E","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 69 |
| Details | Transmembrane: {"description":"Helical; Name=Helix F","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 84 |
| Details | Transmembrane: {"description":"Helical; Name=Helix G","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
