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 | 12 |
| Details | binding site for residue RET A 300 |
| Chain | Residue |
| A | TRP96 |
| A | TRP199 |
| A | ASP222 |
| A | LYS226 |
| A | THR100 |
| A | LEU103 |
| A | TRP148 |
| A | SER151 |
| A | THR152 |
| A | TRP192 |
| A | TYR195 |
| A | PRO196 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue R16 A 302 |
| Chain | Residue |
| A | ILE25 |
| A | THR120 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue R16 A 303 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue R16 A 304 |
| Chain | Residue |
| A | LEU29 |
| A | TYR36 |
| A | THR224 |
| A | VAL227 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue R16 A 305 |
| Chain | Residue |
| A | ASP114 |
| A | THR117 |
| A | THR120 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue DD9 A 308 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue DD9 A 309 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue DD9 A 310 |
| Chain | Residue |
| A | ALA65 |
| A | LEU68 |
| A | PHE72 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue DD9 A 312 |
| Chain | Residue |
| A | LEU58 |
| A | ILE197 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue R16 A 314 |
| Chain | Residue |
| A | SER146 |
| A | PHE150 |
| site_id | AD2 |
| 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 | AD3 |
| 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 | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 715 |
| Chain | Residue |
| A | PCA7 |
| A | ALA8 |
| A | GLY210 |
| A | GLY212 |
| A | ILE213 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 716 |
| Chain | Residue |
| A | LYS47 |
| A | HOH575 |
| A | HOH586 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 717 |
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 | 21 |
| Details | Transmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 27 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=Helix C","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=Helix D","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=Helix E","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=Helix F","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=Helix G","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
