1P8I
F219L BACTERIORHODOPSIN MUTANT
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 | 0015454 | molecular_function | light-driven active monoatomic ion transmembrane transporter activity |
A | 0016020 | cellular_component | membrane |
A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE RET A 301 |
Chain | Residue |
A | TRP86 |
A | LYS216 |
A | THR90 |
A | MET118 |
A | SER141 |
A | THR142 |
A | TRP182 |
A | TYR185 |
A | TRP189 |
A | ASP212 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LI1 A 601 |
Chain | Residue |
A | ILE11 |
A | ILE140 |
A | LI1606 |
A | LI1608 |
A | SQU701 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LI1 A 602 |
Chain | Residue |
A | TRP12 |
A | TYR131 |
A | PHE135 |
A | ALA139 |
A | SER162 |
A | MET163 |
A | ARG164 |
A | PRO165 |
A | ALA196 |
A | ASN202 |
A | ILE203 |
A | LEU207 |
A | LI1608 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LI1 A 603 |
Chain | Residue |
A | LEU190 |
A | ILE198 |
A | PRO200 |
A | LI1604 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LI1 A 604 |
Chain | Residue |
A | ILE198 |
A | LI1603 |
A | LI1610 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE LI1 A 605 |
Chain | Residue |
A | LI1611 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LI1 A 606 |
Chain | Residue |
A | ALA18 |
A | LEU22 |
A | LI1601 |
A | LI1611 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LI1 A 607 |
Chain | Residue |
A | THR55 |
A | MET56 |
A | TYR64 |
A | TRP80 |
A | TRP80 |
A | ALA84 |
A | PHE88 |
A | GLY116 |
A | LEU127 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LI1 A 608 |
Chain | Residue |
A | LI1601 |
A | LI1602 |
A | SQU701 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LI1 A 609 |
Chain | Residue |
A | PHE154 |
A | ASN176 |
A | LI1610 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LI1 A 610 |
Chain | Residue |
A | PHE153 |
A | LYS172 |
A | ASN176 |
A | VAL179 |
A | VAL180 |
A | SER183 |
A | VAL187 |
A | LI1604 |
A | LI1609 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE LI1 A 611 |
Chain | Residue |
A | LEU22 |
A | LEU25 |
A | TYR26 |
A | VAL29 |
A | LI1605 |
A | LI1606 |
A | SQU701 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LI1 A 612 |
Chain | Residue |
A | LEU25 |
A | LEU28 |
A | ALA44 |
A | THR47 |
A | ALA110 |
A | ALA114 |
A | TYR147 |
A | HOH512 |
A | HOH513 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LI1 A 613 |
Chain | Residue |
A | LEU87 |
A | LEU95 |
A | VAL112 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SQU A 701 |
Chain | Residue |
A | SER214 |
A | VAL217 |
A | GLY218 |
A | LEU221 |
A | LI1601 |
A | LI1608 |
A | LI1611 |
Functional Information from PROSITE/UniProt
site_id | PS00950 |
Number of Residues | 13 |
Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL |
Chain | Residue | Details |
A | ARG82-LEU94 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 41 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | GLN1-GLU9 | |
A | GLY63-TYR79 | |
A | THR128-ARG134 | |
A | GLY192-ILE203 |
site_id | SWS_FT_FI2 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=Helix A => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | TRP10-VAL29 |
site_id | SWS_FT_FI3 |
Number of Residues | 65 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | LYS30-TYR43 | |
A | LEU97-THR107 | |
A | GLY155-LYS172 | |
A | LEU224-ASP249 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=Helix B => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | ALA44-LEU62 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | TRP80-ASP96 |
site_id | SWS_FT_FI6 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=Helix D => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | ILE108-LEU127 |
site_id | SWS_FT_FI7 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=Helix E => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | PHE135-PHE154 |
site_id | SWS_FT_FI8 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=Helix F => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | VAL173-ILE191 |
site_id | SWS_FT_FI9 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=Helix G => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | GLU204-LEU223 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064 |
Chain | Residue | Details |
A | ASP85 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408 |
Chain | Residue | Details |
A | GLN1 |
Chain | Residue | Details |
A | LYS216 |