8CQD
Cryo-EM structure of hexameric proteorhodopsin A18L mutant
Functional Information from PROSITE/UniProt
site_id | PS00950 |
Number of Residues | 13 |
Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYiDWlLTVPLLI |
Chain | Residue | Details |
A | ARG95-ILE107 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 138 |
Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:34226545 |
Chain | Residue | Details |
A | ALA19-TYR29 | |
C | GLY88-SER90 | |
C | GLY145-MET147 | |
C | TYR209-LEU218 | |
E | ALA19-TYR29 | |
E | GLY88-SER90 | |
E | GLY145-MET147 | |
E | TYR209-LEU218 | |
F | ALA19-TYR29 | |
F | GLY88-SER90 | |
F | GLY145-MET147 | |
A | GLY88-SER90 | |
F | TYR209-LEU218 | |
D | ALA19-TYR29 | |
D | GLY88-SER90 | |
D | GLY145-MET147 | |
D | TYR209-LEU218 | |
A | GLY145-MET147 | |
A | TYR209-LEU218 | |
B | ALA19-TYR29 | |
B | GLY88-SER90 | |
B | GLY145-MET147 | |
B | TYR209-LEU218 | |
C | ALA19-TYR29 |
site_id | SWS_FT_FI2 |
Number of Residues | 1116 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:34226545 |
Chain | Residue | Details |
A | THR30-ASP53 | |
B | PRO91-THR118 | |
B | GLY122-ALA144 | |
B | ALA148-ASN177 | |
B | PRO181-GLY208 | |
B | ASN219-ASN249 | |
C | THR30-ASP53 | |
C | TRP59-THR87 | |
C | PRO91-THR118 | |
C | GLY122-ALA144 | |
C | ALA148-ASN177 | |
A | TRP59-THR87 | |
C | PRO181-GLY208 | |
C | ASN219-ASN249 | |
E | THR30-ASP53 | |
E | TRP59-THR87 | |
E | PRO91-THR118 | |
E | GLY122-ALA144 | |
E | ALA148-ASN177 | |
E | PRO181-GLY208 | |
E | ASN219-ASN249 | |
F | THR30-ASP53 | |
A | PRO91-THR118 | |
F | TRP59-THR87 | |
F | PRO91-THR118 | |
F | GLY122-ALA144 | |
F | ALA148-ASN177 | |
F | PRO181-GLY208 | |
F | ASN219-ASN249 | |
D | THR30-ASP53 | |
D | TRP59-THR87 | |
D | PRO91-THR118 | |
D | GLY122-ALA144 | |
A | GLY122-ALA144 | |
D | ALA148-ASN177 | |
D | PRO181-GLY208 | |
D | ASN219-ASN249 | |
A | ALA148-ASN177 | |
A | PRO181-GLY208 | |
A | ASN219-ASN249 | |
B | THR30-ASP53 | |
B | TRP59-THR87 |
site_id | SWS_FT_FI3 |
Number of Residues | 54 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:34226545 |
Chain | Residue | Details |
A | ARG54-LYS58 | |
C | ASN119-ALA121 | |
C | THR178-SER180 | |
C | ALA250 | |
E | ARG54-LYS58 | |
E | ASN119-ALA121 | |
E | THR178-SER180 | |
E | ALA250 | |
F | ARG54-LYS58 | |
F | ASN119-ALA121 | |
F | THR178-SER180 | |
A | ASN119-ALA121 | |
F | ALA250 | |
D | ARG54-LYS58 | |
D | ASN119-ALA121 | |
D | THR178-SER180 | |
D | ALA250 | |
A | THR178-SER180 | |
A | ALA250 | |
B | ARG54-LYS58 | |
B | ASN119-ALA121 | |
B | THR178-SER180 | |
B | ALA250 | |
C | ARG54-LYS58 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Primary proton acceptor => ECO:0000255|PIRSR:PIRSR038142-1, ECO:0000305|PubMed:34226545 |
Chain | Residue | Details |
A | ASP98 | |
B | ASP98 | |
C | ASP98 | |
E | ASP98 | |
F | ASP98 | |
D | ASP98 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | SITE: Responsible for spectral tuning => ECO:0000255|PIRSR:PIRSR038142-1 |
Chain | Residue | Details |
A | LEU106 | |
B | LEU106 | |
C | LEU106 | |
E | LEU106 | |
F | LEU106 | |
D | LEU106 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | SITE: Primary proton donor => ECO:0000255|PIRSR:PIRSR038142-1, ECO:0000305|PubMed:34226545 |
Chain | Residue | Details |
A | GLU109 | |
B | GLU109 | |
C | GLU109 | |
E | GLU109 | |
F | GLU109 | |
D | GLU109 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | SITE: Proton release group => ECO:0000305|PubMed:34226545 |
Chain | Residue | Details |
A | GLU143 | |
B | GLU143 | |
C | GLU143 | |
E | GLU143 | |
F | GLU143 | |
D | GLU143 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:34226545, ECO:0007744|PDB:7B03 |
Chain | Residue | Details |
A | LYS232 | |
B | LYS232 | |
C | LYS232 | |
E | LYS232 | |
F | LYS232 | |
D | LYS232 |