4HYX
Crystal Structure Analysis of the Bacteriorhodopsin in Facial Amphiphile-4 DMPC Bicelle
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 |
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 | 0015454 | molecular_function | light-driven active monoatomic ion transmembrane transporter activity |
B | 0016020 | cellular_component | membrane |
B | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE RET A 301 |
Chain | Residue |
A | TRP86 |
A | ASP212 |
A | LYS216 |
A | THR90 |
A | LEU93 |
A | SER141 |
A | THR142 |
A | TRP182 |
A | TYR185 |
A | PRO186 |
A | TRP189 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE D10 A 303 |
Chain | Residue |
A | D10307 |
B | PHE135 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D10 A 304 |
Chain | Residue |
A | ASN176 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE D10 A 305 |
Chain | Residue |
A | LYS41 |
A | ILE45 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D10 A 306 |
Chain | Residue |
A | GLY106 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D10 A 307 |
Chain | Residue |
A | D10303 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE OCT A 308 |
Chain | Residue |
A | MET145 |
A | SER183 |
A | PRO186 |
B | MET145 |
B | SER183 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE RET B 301 |
Chain | Residue |
B | TRP86 |
B | THR90 |
B | MET118 |
B | TRP138 |
B | SER141 |
B | THR142 |
B | TRP182 |
B | TYR185 |
B | PRO186 |
B | TRP189 |
B | ASP212 |
B | ALA215 |
B | LYS216 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE D10 B 302 |
Chain | Residue |
B | VAL124 |
B | THR128 |
B | LYS129 |
B | TRP137 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE D10 B 303 |
Chain | Residue |
B | LEU95 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE HEX B 304 |
Chain | Residue |
B | GLY106 |
B | LEU109 |
B | ALA110 |
B | C14305 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE C14 B 305 |
Chain | Residue |
B | ILE140 |
B | ALA144 |
B | TYR147 |
B | HEX304 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE OCT B 306 |
Chain | Residue |
B | ASN176 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE D10 B 308 |
Chain | Residue |
A | VAL136 |
A | LEU190 |
site_id | BC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 309 |
Chain | Residue |
B | PRO77 |
B | ILE78 |
B | TYR79 |
B | ARG82 |
B | SER193 |
B | GLU194 |
B | LEU201 |
B | THR205 |
B | HOH411 |
B | HOH415 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 82 |
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 | |
B | GLN1-GLU9 | |
B | GLY63-TYR79 | |
B | THR128-ARG134 | |
B | GLY192-ILE203 |
site_id | SWS_FT_FI2 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Name=Helix A => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | TRP10-VAL29 | |
B | TRP10-VAL29 |
site_id | SWS_FT_FI3 |
Number of Residues | 130 |
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 | |
B | LYS30-TYR43 | |
B | LEU97-THR107 | |
B | GLY155-LYS172 | |
B | LEU224-ASP249 |
site_id | SWS_FT_FI4 |
Number of Residues | 36 |
Details | TRANSMEM: Helical; Name=Helix B => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | ALA44-LEU62 | |
B | ALA44-LEU62 |
site_id | SWS_FT_FI5 |
Number of Residues | 32 |
Details | TRANSMEM: Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | TRP80-ASP96 | |
B | TRP80-ASP96 |
site_id | SWS_FT_FI6 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Name=Helix D => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | ILE108-LEU127 | |
B | ILE108-LEU127 |
site_id | SWS_FT_FI7 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Name=Helix E => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | PHE135-PHE154 | |
B | PHE135-PHE154 |
site_id | SWS_FT_FI8 |
Number of Residues | 36 |
Details | TRANSMEM: Helical; Name=Helix F => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | VAL173-ILE191 | |
B | VAL173-ILE191 |
site_id | SWS_FT_FI9 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Name=Helix G => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
Chain | Residue | Details |
A | GLU204-LEU223 | |
B | GLU204-LEU223 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | SITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064 |
Chain | Residue | Details |
A | ASP85 | |
B | ASP85 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408 |
Chain | Residue | Details |
A | GLN1 | |
B | GLN1 |
Chain | Residue | Details |
A | LYS216 | |
B | LYS216 |