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 | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | GLU16-ALA36 | |
B | TYR91-ALA111 | |
B | ILE116-THR136 | |
B | ALA144-PHE164 | |
B | ILE185-ALA205 | |
B | GLU212-LEU232 | |
C | GLU16-ALA36 | |
C | VAL51-PHE71 | |
C | TYR91-ALA111 | |
C | ILE116-THR136 | |
C | ALA144-PHE164 | |
A | VAL51-PHE71 | |
C | ILE185-ALA205 | |
C | GLU212-LEU232 | |
A | TYR91-ALA111 | |
A | ILE116-THR136 | |
A | ALA144-PHE164 | |
A | ILE185-ALA205 | |
A | GLU212-LEU232 | |
B | GLU16-ALA36 | |
B | VAL51-PHE71 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | SITE: Primary proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP93 | |
B | ASP93 | |
C | ASP93 | |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250 |
Chain | Residue | Details |
A | GLN7 | |
B | GLN7 | |
C | GLN7 | |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: N6-(retinylidene)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS224 | |
B | LYS224 | |
C | LYS224 | |