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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | THR111 |
| A | SER115 |
| A | LYS242 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RET A 999 |
| Chain | Residue |
| A | SER168 |
| A | PHE172 |
| A | TRP207 |
| A | TYR210 |
| A | PRO211 |
| A | ASP238 |
| A | LYS242 |
| A | TRP112 |
| A | THR116 |
| A | MET144 |
| A | TYR165 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PLM A 700 |
| Chain | Residue |
| A | SER75 |
| A | LEU110 |
| A | THR111 |
| A | PRO117 |
| A | PHE135 |
| A | ALA139 |
| A | VAL146 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC A 701 |
| Chain | Residue |
| A | TRP162 |
| A | HOH2064 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC A 703 |
| Chain | Residue |
| A | OLC705 |
| A | OLC719 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLC A 705 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 709 |
| Chain | Residue |
| A | ALA157 |
| A | LEU159 |
| A | PHE160 |
| A | OLC717 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLC A 711 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 713 |
| Chain | Residue |
| A | GLY41 |
| A | ILE42 |
| A | LEU45 |
| A | OLC715 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 715 |
| Chain | Residue |
| A | VAL37 |
| A | ALA38 |
| A | LEU45 |
| A | OLC713 |
| A | OLC717 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC A 717 |
| Chain | Residue |
| A | ARG52 |
| A | OLC709 |
| A | OLC715 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLC A 719 |
Functional Information from PROSITE/UniProt
| site_id | PS00327 |
| Number of Residues | 12 |
| Details | BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. YSVLDVfAKyVF |
| Chain | Residue | Details |
| A | TYR234-PHE245 | |
| site_id | PS00950 |
| Number of Residues | 13 |
| Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYlTWaLSTPMIL |
| Chain | Residue | Details |
| A | ARG108-LEU120 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 34 |
| 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 | 23 |
| Details | Transmembrane: {"description":"Helical; Name=Helix D","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=Helix E","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=Helix F","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 28 |
| 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"}]} |
