2HHK
Reaction centre from Rhodobacter sphaeroides strain R-26.1 complexed with dibrominated phosphatidylglycerol
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 | 5 |
Details | BINDING SITE FOR RESIDUE K H 700 |
Chain | Residue |
H | HOH1370 |
H | MET134 |
H | ALA137 |
H | PHE140 |
H | HOH1369 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL M 701 |
Chain | Residue |
M | SER36 |
M | THR37 |
M | LEU38 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 M 702 |
Chain | Residue |
M | TYR3 |
M | GLN4 |
M | ASN5 |
M | ILE6 |
M | PHE7 |
M | HOH1410 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 M 703 |
Chain | Residue |
M | ASN28 |
M | GLY53 |
M | SER54 |
M | HOH1182 |
M | HOH1188 |
M | HOH1310 |
M | HOH1312 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PO4 H 704 |
Chain | Residue |
H | ARG202 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 M 705 |
Chain | Residue |
M | GLN138 |
M | HOH1155 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BCL M 311 |
Chain | Residue |
L | HIS168 |
L | MET174 |
L | ILE177 |
L | SER178 |
L | THR182 |
L | U10502 |
M | MET122 |
M | ILE179 |
M | HIS182 |
M | LEU183 |
M | THR186 |
M | BCL313 |
M | BPH401 |
M | PGK802 |
M | LDA920 |
M | HOH1006 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BCL L 312 |
Chain | Residue |
L | PHE97 |
L | ALA127 |
L | LEU131 |
L | VAL157 |
L | TYR162 |
L | ASN166 |
L | PHE167 |
L | HIS168 |
L | HIS173 |
L | ALA176 |
L | ILE177 |
L | PHE180 |
L | SER244 |
L | CYS247 |
L | MET248 |
L | BCL314 |
L | BPH402 |
M | TYR210 |
M | BCL313 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE BCL M 313 |
Chain | Residue |
L | VAL157 |
L | TYR162 |
L | BCL312 |
M | ALA153 |
M | LEU160 |
M | THR186 |
M | ASN187 |
M | SER190 |
M | LEU196 |
M | PHE197 |
M | HIS202 |
M | SER205 |
M | ILE206 |
M | TYR210 |
M | VAL276 |
M | GLY280 |
M | ILE284 |
M | BCL311 |
M | BPH401 |
M | PGK802 |
site_id | BC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BCL L 314 |
Chain | Residue |
H | PGT801 |
L | TYR128 |
L | PHE146 |
L | ILE150 |
L | HIS153 |
L | LEU154 |
L | BCL312 |
L | BPH402 |
L | HOH1023 |
M | PHE197 |
M | GLY203 |
M | ILE206 |
M | ALA207 |
M | TYR210 |
M | U10501 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BPH M 401 |
Chain | Residue |
L | PHE181 |
L | LEU185 |
L | LEU189 |
M | GLY63 |
M | ALA125 |
M | TRP129 |
M | THR146 |
M | ALA149 |
M | PHE150 |
M | ALA153 |
M | THR277 |
M | BCL311 |
M | BCL313 |
site_id | BC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BPH L 402 |
Chain | Residue |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | ILE117 |
L | ALA120 |
L | PHE121 |
L | ALA124 |
L | TYR148 |
L | GLY149 |
L | HIS153 |
L | LEU238 |
L | VAL241 |
L | BCL312 |
L | BCL314 |
M | TYR210 |
M | ALA213 |
M | LEU214 |
M | TRP252 |
M | MET256 |
site_id | BC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE U10 M 501 |
Chain | Residue |
L | TYR30 |
L | ARG103 |
L | BCL314 |
M | MET218 |
M | HIS219 |
M | THR222 |
M | ALA248 |
M | ALA249 |
M | TRP252 |
M | MET256 |
M | ASN259 |
M | ALA260 |
M | MET262 |
M | ILE265 |
M | TRP268 |
M | MET272 |
site_id | BC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE U10 L 502 |
Chain | Residue |
L | SER178 |
L | PHE179 |
L | THR182 |
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 | BCL311 |
M | PGK802 |
site_id | BC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CDL M 800 |
Chain | Residue |
H | TYR30 |
H | LDA904 |
H | HOH1211 |
L | ASN199 |
L | PRO200 |
M | GLY143 |
M | LYS144 |
M | HIS145 |
M | TRP148 |
M | ARG267 |
M | ILE270 |
M | TRP271 |
M | LEU278 |
M | HOH1197 |
site_id | BC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PGT H 801 |
Chain | Residue |
H | TRP21 |
H | LDA901 |
H | LDA903 |
H | HOH1407 |
H | HOH1408 |
H | HOH1409 |
L | PRO61 |
L | GLN62 |
L | TYR148 |
L | BCL314 |
M | TRP271 |
M | MET272 |
site_id | BC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PGK M 802 |
Chain | Residue |
L | VAL220 |
L | GLY221 |
L | U10502 |
M | LEU26 |
M | ALA27 |
M | ARG29 |
M | GLY31 |
M | GLY33 |
M | LEU47 |
M | GLY48 |
M | TRP129 |
M | BCL311 |
M | BCL313 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LDA H 901 |
Chain | Residue |
H | TYR40 |
H | PHE56 |
H | PGT801 |
H | LDA903 |
M | ARG253 |
M | PHE258 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA M 902 |
Chain | Residue |
H | LDA903 |
H | HOH1161 |
M | GLY257 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA H 903 |
Chain | Residue |
H | TYR18 |
H | PGT801 |
H | LDA901 |
H | LDA904 |
M | LDA902 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA H 904 |
Chain | Residue |
H | ALA25 |
H | LDA903 |
M | CDL800 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA M 907 |
Chain | Residue |
M | PHE7 |
M | SER8 |
M | TRP41 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LDA M 920 |
Chain | Residue |
M | TRP115 |
M | GLY161 |
M | ALA174 |
M | VAL175 |
M | PRO176 |
M | BCL311 |
site_id | CC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL H 706 |
Chain | Residue |
H | ARG177 |
H | PHE178 |
H | PRO192 |
H | GLN194 |
H | GLU230 |
H | CYS234 |
M | SER227 |
M | ARG228 |
M | GLY230 |
M | ARG233 |
site_id | CC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL L 707 |
Chain | Residue |
L | SER52 |
L | SER65 |
L | TYR67 |
L | LEU80 |
L | ALA81 |
L | LEU85 |
L | HOH1093 |
L | HOH1285 |
site_id | CC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL L 708 |
Chain | Residue |
H | THR63 |
H | PHE64 |
L | ALA198 |
L | ASN199 |
L | PRO200 |
L | HOH1096 |
L | HOH1184 |
L | HOH1334 |
M | HOH1197 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL L 709 |
Chain | Residue |
H | LEU241 |
L | CYS108 |
L | GLY112 |
L | ILE113 |
L | TYR115 |
L | HOH1102 |
M | GLU2 |
M | ARG228 |
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 |