1RG5
Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1
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 500 |
Chain | Residue |
L | HIS190 |
L | HIS230 |
M | HIS219 |
M | GLU234 |
M | HIS266 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BCL M 501 |
Chain | Residue |
L | THR182 |
L | U10502 |
L | HOH709 |
M | MET122 |
M | ILE179 |
M | HIS182 |
M | LEU183 |
M | THR186 |
M | BPH401 |
M | BCL502 |
M | LDA905 |
M | LDA920 |
L | HIS168 |
L | MET174 |
L | ILE177 |
L | SER178 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BCL L 302 |
Chain | Residue |
L | PHE97 |
L | ALA124 |
L | VAL157 |
L | PHE167 |
L | HIS168 |
L | HIS173 |
L | ILE177 |
L | SER244 |
L | MET248 |
L | BCL304 |
L | BPH402 |
M | BCL502 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BCL M 502 |
Chain | Residue |
L | BCL302 |
M | ALA153 |
M | THR186 |
M | ASN187 |
M | LEU196 |
M | PHE197 |
M | HIS202 |
M | SER205 |
M | ILE206 |
M | TYR210 |
M | GLY280 |
M | ILE284 |
M | BPH401 |
M | BCL501 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BCL L 304 |
Chain | Residue |
L | HIS153 |
L | LEU154 |
L | BCL302 |
L | BPH402 |
M | GLY203 |
M | ILE206 |
M | ALA207 |
M | TYR210 |
M | LDA902 |
M | HOH925 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BPH M 401 |
Chain | Residue |
L | PHE181 |
L | LEU189 |
M | PHE67 |
M | TRP129 |
M | PHE150 |
M | ALA153 |
M | ALA273 |
M | THR277 |
M | BCL501 |
M | BCL502 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BPH L 402 |
Chain | Residue |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | PHE121 |
L | BCL302 |
L | BCL304 |
M | TYR210 |
M | LEU214 |
M | MET256 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE U10 M 503 |
Chain | Residue |
L | THR38 |
L | ARG103 |
M | HIS219 |
M | THR222 |
M | ALA249 |
M | TRP252 |
M | ASN259 |
M | ALA260 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE U10 L 502 |
Chain | Residue |
L | SER178 |
L | LEU189 |
L | HIS190 |
L | LEU193 |
L | GLU212 |
L | ASP213 |
L | PHE216 |
L | TYR222 |
L | SER223 |
L | ILE224 |
L | GLY225 |
L | THR226 |
L | ILE229 |
M | BCL501 |
M | LDA907 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE HTO M 706 |
Chain | Residue |
M | THR289 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE HTO L 707 |
Chain | Residue |
L | PRO118 |
L | ALA122 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CDL M 800 |
Chain | Residue |
H | TYR30 |
H | HOH936 |
L | ASN199 |
L | PRO200 |
M | GLY143 |
M | LYS144 |
M | HIS145 |
M | TRP148 |
M | ARG267 |
M | HOH957 |
M | HOH970 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA H 901 |
Chain | Residue |
H | TYR40 |
M | ARG253 |
M | GLY257 |
M | LDA902 |
M | LDA903 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE LDA M 902 |
Chain | Residue |
H | LDA901 |
L | BCL304 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE LDA M 903 |
Chain | Residue |
H | LDA901 |
M | GLY257 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE LDA M 905 |
Chain | Residue |
M | VAL32 |
M | BCL501 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE LDA M 907 |
Chain | Residue |
L | U10502 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE LDA M 920 |
Chain | Residue |
M | TRP115 |
M | GLY161 |
M | VAL175 |
M | PRO176 |
M | GLY178 |
M | ILE179 |
M | BCL501 |
M | HOH964 |
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 | ASN195-ALA221 |
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 | GLU111-LEU140 | |
M | GLY143-MET168 | |
M | TYR198-VAL226 | |
M | ALA260-LEU286 |
site_id | SWS_FT_FI2 |
Number of Residues | 19 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
H | LEU12-LEU31 | |
M | GLY203 | |
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 | LEU235 | |
M | ARG253 | |
M | ARG267 |
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 |