2RCR
STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES
Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0015979 | biological_process | photosynthesis |
H | 0016020 | cellular_component | membrane |
H | 0019684 | biological_process | photosynthesis, light reaction |
H | 0030077 | cellular_component | plasma membrane light-harvesting complex |
H | 0042314 | molecular_function | bacteriochlorophyll binding |
H | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
H | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
L | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
L | 0015979 | biological_process | photosynthesis |
L | 0016020 | cellular_component | membrane |
L | 0019684 | biological_process | photosynthesis, light reaction |
L | 0030077 | cellular_component | plasma membrane light-harvesting complex |
L | 0042314 | molecular_function | bacteriochlorophyll binding |
L | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
L | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
L | 0046872 | molecular_function | metal ion binding |
M | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
M | 0015979 | biological_process | photosynthesis |
M | 0016020 | cellular_component | membrane |
M | 0019684 | biological_process | photosynthesis, light reaction |
M | 0030077 | cellular_component | plasma membrane light-harvesting complex |
M | 0042314 | molecular_function | bacteriochlorophyll binding |
M | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
M | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
M | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE M 600 |
Chain | Residue |
L | HIS190 |
L | HIS230 |
M | HIS217 |
M | GLU232 |
M | HIS264 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BCL M 601 |
Chain | Residue |
L | BCL350 |
M | LEU158 |
M | VAL173 |
M | HIS180 |
M | TRP183 |
M | THR184 |
M | BCL400 |
M | BPH500 |
L | HIS168 |
L | MET174 |
L | ILE177 |
L | SER178 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BCL L 350 |
Chain | Residue |
L | PHE97 |
L | ALA124 |
L | ALA127 |
L | TYR128 |
L | TRP156 |
L | VAL157 |
L | TYR162 |
L | HIS168 |
L | HIS173 |
L | ILE177 |
L | PHE180 |
L | VAL241 |
L | SER244 |
L | MET248 |
L | BCL450 |
L | BPH550 |
M | TYR208 |
M | BCL400 |
M | BCL601 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE BCL M 400 |
Chain | Residue |
L | PHE181 |
L | BCL350 |
L | BCL450 |
M | ALA151 |
M | LEU154 |
M | LEU158 |
M | THR184 |
M | PHE187 |
M | SER188 |
M | LEU194 |
M | PHE195 |
M | HIS200 |
M | SER203 |
M | ILE204 |
M | TYR208 |
M | THR275 |
M | GLY278 |
M | ILE282 |
M | BPH500 |
M | BCL601 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BCL L 450 |
Chain | Residue |
L | TYR128 |
L | PHE146 |
L | HIS153 |
L | BCL350 |
L | BPH550 |
M | PHE195 |
M | ALA205 |
M | PHE206 |
M | BCL400 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BPH M 500 |
Chain | Residue |
L | PHE181 |
L | LEU185 |
L | LEU189 |
L | UQ800 |
M | SER58 |
M | PHE66 |
M | TRP127 |
M | THR131 |
M | THR144 |
M | ALA147 |
M | PHE148 |
M | ALA271 |
M | BCL400 |
M | BCL601 |
site_id | AC7 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE BPH L 550 |
Chain | Residue |
L | PHE41 |
L | ALA42 |
L | GLY45 |
L | ILE49 |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | ILE117 |
L | PHE121 |
L | TYR148 |
L | ILE150 |
L | SER237 |
L | BCL350 |
L | BCL450 |
M | TYR208 |
M | ALA211 |
M | LEU212 |
M | MET216 |
M | TRP250 |
M | MET254 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE UQ M 750 |
Chain | Residue |
M | LEU212 |
M | MET216 |
M | THR220 |
M | ILE221 |
M | ALA243 |
M | TRP250 |
M | MET254 |
M | PHE256 |
M | ALA258 |
M | THR259 |
M | MET260 |
M | ILE263 |
M | TRP266 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE UQ L 800 |
Chain | Residue |
L | LEU185 |
L | HIS190 |
L | LEU193 |
L | GLU212 |
L | PHE216 |
L | VAL220 |
L | SER223 |
L | ILE224 |
L | ILE229 |
M | TRP127 |
M | BPH500 |
Functional Information from PROSITE/UniProt
site_id | PS00244 |
Number of Residues | 27 |
Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NfhynPaHmiAisffftnalalAlHGA |
Chain | Residue | Details |
L | ASN166-ALA192 | |
M | ASN193-ALA219 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | TOPO_DOM: Periplasmic |
Chain | Residue | Details |
H | MET1-ASP11 | |
M | GLU109-LEU138 | |
M | GLY141-MET166 | |
M | TYR196-VAL224 | |
M | ALA258-LEU284 |
site_id | SWS_FT_FI2 |
Number of Residues | 19 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
H | LEU12-LEU31 | |
M | GLY201 | |
L | ILE117-MET139 | |
L | ALA172-ASN199 | |
L | THR226-THR251 |
site_id | SWS_FT_FI3 |
Number of Residues | 228 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
H | GLN32-ALA260 | |
M | LEU233 | |
M | ARG251 | |
M | ARG265 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
L | LEU154 | |
L | MET174 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
L | GLY191 | |
L | ARG217 | |
L | ARG231 |