3HAP
Crystal structure of bacteriorhodopsin mutant L111A crystallized from bicelles
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 | 12 |
Details | BINDING SITE FOR RESIDUE RET A 301 |
Chain | Residue |
A | TRP86 |
A | ASP212 |
A | ALA215 |
A | LYS216 |
A | THR90 |
A | TRP138 |
A | SER141 |
A | THR142 |
A | TRP182 |
A | TYR185 |
A | PRO186 |
A | TRP189 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D12 A 402 |
Chain | Residue |
A | D12403 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D12 A 403 |
Chain | Residue |
A | D12402 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D12 A 405 |
Chain | Residue |
A | ASN176 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE D10 A 406 |
Chain | Residue |
A | THR17 |
A | ALA44 |
A | D12251 |
A | D12256 |
A | CPS501 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE R16 A 411 |
Chain | Residue |
A | VAL136 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CPS A 501 |
Chain | Residue |
A | GLY6 |
A | LYS41 |
A | LEU61 |
A | GLN105 |
A | ILE108 |
A | HOH298 |
A | HOH329 |
A | HOH351 |
A | D10406 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D10 A 250 |
Chain | Residue |
A | LEU25 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE D12 A 251 |
Chain | Residue |
A | LEU15 |
A | D10406 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D12 A 254 |
Chain | Residue |
A | HOH375 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D12 A 255 |
Chain | Residue |
A | ALA110 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE D12 A 256 |
Chain | Residue |
A | LEU28 |
A | LEU48 |
A | D10406 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D10 A 257 |
Chain | Residue |
A | ILE203 |
Functional Information from PROSITE/UniProt
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 |