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 |
| C | 0005216 | molecular_function | monoatomic ion channel activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0007602 | biological_process | phototransduction |
| C | 0009881 | molecular_function | photoreceptor activity |
| C | 0016020 | cellular_component | membrane |
| C | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue OLC A 301 |
| Chain | Residue |
| A | GLU48 |
| B | GLY117 |
| B | ALA118 |
| B | PHE125 |
| B | VAL128 |
| B | OLC301 |
| A | VAL51 |
| A | ILE52 |
| A | LEU55 |
| A | ILE59 |
| A | ALA89 |
| A | LEU103 |
| A | OLC303 |
| B | ARG114 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue OLB A 302 |
| Chain | Residue |
| A | ILE122 |
| A | PHE125 |
| A | PHE155 |
| A | TYR159 |
| C | THR24 |
| C | ILE35 |
| C | VAL51 |
| C | LEU55 |
| C | ALA61 |
| C | HOH423 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 303 |
| Chain | Residue |
| A | PRO99 |
| A | LEU103 |
| A | LEU107 |
| A | GLN113 |
| A | ILE116 |
| A | OLC301 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue RET A 304 |
| Chain | Residue |
| A | TRP94 |
| A | THR97 |
| A | THR98 |
| A | MET126 |
| A | TRP146 |
| A | SER149 |
| A | THR150 |
| A | TRP190 |
| A | TYR193 |
| A | ALA223 |
| A | LYS224 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue OLC B 301 |
| Chain | Residue |
| A | OLC301 |
| B | LEU100 |
| B | GLN113 |
| B | ILE116 |
| B | ALA124 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue OLC B 302 |
| Chain | Residue |
| B | VAL154 |
| B | LEU157 |
| B | TYR158 |
| B | VAL161 |
| B | ALA162 |
| B | GLY165 |
| B | GLU166 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue OLB B 303 |
| Chain | Residue |
| B | THR24 |
| B | LEU28 |
| B | MET31 |
| B | LYS47 |
| B | ILE54 |
| B | LEU55 |
| B | ALA58 |
| B | LEU65 |
| B | HOH403 |
| B | HOH421 |
| C | ILE122 |
| C | PHE125 |
| C | ILE148 |
| C | SER152 |
| C | PHE155 |
| C | TYR159 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue OLC C 301 |
| Chain | Residue |
| B | PHE96 |
| C | LEU95 |
| C | PRO99 |
| C | LEU107 |
| C | ALA111 |
| C | SER112 |
| C | GLN113 |
| C | OLB303 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue OLC C 302 |
| Chain | Residue |
| B | GLU48 |
| B | VAL51 |
| B | ILE59 |
| C | ARG114 |
| C | ASP115 |
| C | GLY117 |
| C | ALA118 |
| C | ALA124 |
| C | VAL128 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue OLB C 303 |
| Chain | Residue |
| A | GLY117 |
| A | GLY121 |
| A | VAL128 |
| C | GLU48 |
| C | ILE59 |
| C | PHE96 |
| C | LEU100 |
| C | LEU103 |
| C | OLC301 |
| C | HOH414 |
| C | HOH415 |
Functional Information from PROSITE/UniProt
| site_id | PS00327 |
| Number of Residues | 12 |
| Details | BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDLvAKvGF |
| Chain | Residue | Details |
| A | PHE216-PHE227 | |
| site_id | PS00950 |
| Number of Residues | 13 |
| Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL |
| Chain | Residue | Details |
| A | ARG90-LEU102 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 420 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Site: {"description":"Primary proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |