4H99
Bacterial Photosynthetic Reaction Center from Rhodobacter sphaeroides with ILE M265 replaced with THR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016168 | molecular_function | chlorophyll binding |
| 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 |
| L | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| L | 0015979 | biological_process | photosynthesis |
| L | 0016168 | molecular_function | chlorophyll binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| M | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| M | 0015979 | biological_process | photosynthesis |
| M | 0016168 | molecular_function | chlorophyll binding |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BCL L 301 |
| Chain | Residue |
| L | PHE97 |
| L | HIS173 |
| L | ALA176 |
| L | ILE177 |
| L | PHE180 |
| L | SER244 |
| L | ALA245 |
| L | CYS247 |
| L | MET248 |
| L | BCL302 |
| L | BPH303 |
| L | ALA124 |
| M | TYR210 |
| M | BCL403 |
| L | ILE125 |
| L | ALA127 |
| L | LEU131 |
| L | TYR162 |
| L | ASN166 |
| L | PHE167 |
| L | HIS168 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCL L 302 |
| Chain | Residue |
| L | TYR128 |
| L | PHE146 |
| L | ILE150 |
| L | HIS153 |
| L | LEU154 |
| L | BCL301 |
| L | BPH303 |
| M | GLY203 |
| M | ILE206 |
| M | ALA207 |
| M | TYR210 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BPH L 303 |
| Chain | Residue |
| L | ALA93 |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | PHE121 |
| L | ALA124 |
| L | TYR148 |
| L | LEU238 |
| L | VAL241 |
| L | BCL301 |
| L | BCL302 |
| M | TYR210 |
| M | ALA213 |
| M | LEU214 |
| M | TRP252 |
| M | MET256 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE U10 L 304 |
| Chain | Residue |
| L | LEU189 |
| L | HIS190 |
| L | LEU193 |
| L | PHE216 |
| L | SER223 |
| L | ILE224 |
| L | GLY225 |
| L | THR226 |
| L | ILE229 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCL M 401 |
| Chain | Residue |
| L | HIS168 |
| L | MET174 |
| L | SER178 |
| L | PHE181 |
| L | THR182 |
| M | HIS182 |
| M | LEU183 |
| M | THR186 |
| M | BCL403 |
| M | BPH404 |
| M | SPO406 |
| M | HOH504 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 402 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS219 |
| M | GLU234 |
| M | HIS266 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BCL M 403 |
| Chain | Residue |
| L | PHE181 |
| L | BCL301 |
| M | ALA153 |
| M | LEU156 |
| 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 | BCL401 |
| M | BPH404 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BPH M 404 |
| Chain | Residue |
| M | VAL126 |
| M | TRP129 |
| M | ALA149 |
| M | PHE150 |
| M | ALA153 |
| M | BCL401 |
| M | BCL403 |
| L | PHE181 |
| L | ALA184 |
| L | LEU185 |
| L | LEU189 |
| M | GLY63 |
| M | PHE67 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE U10 M 405 |
| Chain | Residue |
| M | HIS219 |
| M | THR222 |
| M | ALA248 |
| M | ALA249 |
| M | TRP252 |
| M | MET256 |
| M | ASN259 |
| M | ALA260 |
| M | THR265 |
| M | TRP268 |
| M | MET272 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SPO M 406 |
| Chain | Residue |
| M | ILE70 |
| M | TRP75 |
| M | SER119 |
| M | TRP157 |
| M | GLY161 |
| M | PHE162 |
| M | ILE179 |
| M | HIS182 |
| M | BCL401 |
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 | 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 |
