5B35
Serial Femtosecond Crystallography (SFX) of Ground State Bacteriorhodopsin Crystallized from Bicelles Determined Using 7-keV X-ray Free Electron Laser (XFEL) at SACLA
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 | 0019904 | molecular_function | protein domain specific binding |
A | 0034220 | biological_process | monoatomic ion 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 | TRP189 |
A | ALA215 |
A | LYS216 |
A | THR89 |
A | THR90 |
A | LEU93 |
A | TRP138 |
A | SER141 |
A | THR142 |
A | TRP182 |
A | TYR185 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue 4QM A 302 |
Chain | Residue |
A | LEU61 |
A | LEU99 |
A | ALA103 |
A | ILE108 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue OCT A 303 |
Chain | Residue |
A | D10307 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue D10 A 304 |
Chain | Residue |
A | ARG225 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue D12 A 305 |
Chain | Residue |
A | ILE203 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue D10 A 307 |
Chain | Residue |
A | ILE198 |
A | OCT303 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue R16 A 309 |
Chain | Residue |
A | SER132 |
A | VAL136 |
A | HOH428 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue D10 A 310 |
Chain | Residue |
A | D12315 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue HP6 A 312 |
Chain | Residue |
A | LYS30 |
A | GLY65 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue D12 A 314 |
Chain | Residue |
A | TYR147 |
A | DD9316 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue D12 A 315 |
Chain | Residue |
A | ALA44 |
A | D10310 |
A | R16317 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue DD9 A 316 |
Chain | Residue |
A | GLY106 |
A | LEU109 |
A | D12314 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue R16 A 317 |
Chain | Residue |
A | TRP10 |
A | ILE11 |
A | D12315 |
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 |