2BNP
Lipidic cubic phase grown reaction centre from Rhodobacter sphaeroides, ground state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016020 | cellular_component | membrane |
| A | 0016168 | molecular_function | chlorophyll binding |
| A | 0019684 | biological_process | photosynthesis, light reaction |
| A | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| A | 0042314 | molecular_function | bacteriochlorophyll binding |
| A | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0016168 | molecular_function | chlorophyll binding |
| B | 0019684 | biological_process | photosynthesis, light reaction |
| B | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| B | 0042314 | molecular_function | bacteriochlorophyll binding |
| B | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016020 | cellular_component | membrane |
| C | 0016168 | molecular_function | chlorophyll binding |
| C | 0019684 | biological_process | photosynthesis, light reaction |
| C | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| C | 0042314 | molecular_function | bacteriochlorophyll binding |
| C | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 1305 |
| Chain | Residue |
| A | HIS190 |
| A | HIS230 |
| B | HIS219 |
| B | GLU234 |
| B | HIS266 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1308 |
| Chain | Residue |
| B | PO41309 |
| A | ASN199 |
| A | LYS202 |
| B | HIS145 |
| B | ARG267 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1309 |
| Chain | Residue |
| A | LYS202 |
| B | GLY143 |
| B | LYS144 |
| B | TRP148 |
| B | PO41308 |
| B | HOH2022 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1307 |
| Chain | Residue |
| B | GLY56 |
| B | ARG136 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BCL A 1282 |
| Chain | Residue |
| A | PHE97 |
| A | ALA127 |
| A | LEU131 |
| A | VAL157 |
| A | THR160 |
| A | TYR162 |
| A | ASN166 |
| A | HIS168 |
| A | HIS173 |
| A | ILE177 |
| A | PHE180 |
| A | SER244 |
| A | CYS247 |
| A | MET248 |
| A | BCL1283 |
| A | BPH1284 |
| B | BCL1302 |
| B | BCL1303 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCL A 1283 |
| Chain | Residue |
| A | ILE49 |
| A | TYR128 |
| A | LEU131 |
| A | PHE146 |
| A | ILE150 |
| A | HIS153 |
| A | LEU154 |
| A | BCL1282 |
| A | BPH1284 |
| B | PHE197 |
| B | GLY203 |
| B | ILE206 |
| B | ALA207 |
| B | TYR210 |
| B | LEU214 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BPH A 1284 |
| Chain | Residue |
| A | PHE97 |
| A | TRP100 |
| A | GLU104 |
| A | ILE117 |
| A | PHE121 |
| A | ALA124 |
| A | TYR148 |
| A | VAL241 |
| A | BCL1282 |
| A | BCL1283 |
| B | TYR210 |
| B | ALA213 |
| B | LEU214 |
| B | TRP252 |
| B | MET256 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MST A 1285 |
| Chain | Residue |
| A | HIS190 |
| A | LEU193 |
| A | ASP213 |
| A | PHE216 |
| A | TYR222 |
| A | SER223 |
| A | ILE224 |
| A | GLY225 |
| A | ILE229 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCL B 1302 |
| Chain | Residue |
| A | HIS168 |
| A | MET174 |
| A | ILE177 |
| A | SER178 |
| A | THR182 |
| A | LEU185 |
| A | BCL1282 |
| A | HOH2012 |
| B | TRP157 |
| B | ILE179 |
| B | HIS182 |
| B | LEU183 |
| B | THR186 |
| B | BCL1303 |
| B | BPH1304 |
| site_id | BC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BCL B 1303 |
| Chain | Residue |
| B | PHE189 |
| B | LEU196 |
| B | PHE197 |
| B | HIS202 |
| B | SER205 |
| B | ILE206 |
| B | TYR210 |
| B | VAL276 |
| B | GLY280 |
| B | ILE284 |
| B | BCL1302 |
| B | BPH1304 |
| A | VAL157 |
| A | TYR162 |
| A | PHE181 |
| A | BCL1282 |
| B | ALA153 |
| B | LEU156 |
| B | LEU160 |
| B | THR186 |
| B | ASN187 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BPH B 1304 |
| Chain | Residue |
| A | PHE181 |
| A | LEU185 |
| A | LEU189 |
| A | LEU219 |
| B | GLY63 |
| B | ALA125 |
| B | TRP129 |
| B | THR146 |
| B | PHE150 |
| B | ALA273 |
| B | THR277 |
| B | BCL1302 |
| B | BCL1303 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE U10 B 1306 |
| Chain | Residue |
| B | HIS219 |
| B | THR222 |
| B | ALA248 |
| B | ALA249 |
| B | TRP252 |
| B | MET256 |
| B | PHE258 |
| B | ASN259 |
| B | ALA260 |
| B | THR261 |
| B | ILE265 |
| B | TRP268 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NfhynPaHmiAisffftnalalAlHGA |
| Chain | Residue | Details |
| A | ASN166-ALA192 | |
| B | ASN195-ALA221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 278 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 87 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Binding site: {} |
| Chain | Residue | Details |
