3V3Y
Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV
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 | 8 | 
| Details | BINDING SITE FOR RESIDUE LDA H 702 | 
| Chain | Residue | 
| H | GLN32 | 
| H | TYR40 | 
| H | GLY54 | 
| H | PHE56 | 
| M | ARG253 | 
| M | U10501 | 
| M | LDA701 | 
| M | LDA707 | 
| site_id | AC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE LDA H 704 | 
| Chain | Residue | 
| H | GLY26 | 
| H | LEU27 | 
| H | TYR30 | 
| M | LDA703 | 
| M | PO4800 | 
| H | PHE23 | 
| site_id | AC3 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE LDA H 709 | 
| Chain | Residue | 
| H | TRP21 | 
| site_id | AC4 | 
| Number of Residues | 20 | 
| Details | BINDING SITE FOR RESIDUE BCL L 302 | 
| Chain | Residue | 
| L | PHE97 | 
| L | ALA124 | 
| L | ILE125 | 
| L | ALA127 | 
| L | LEU131 | 
| L | VAL157 | 
| L | TYR162 | 
| L | ASN166 | 
| L | PHE167 | 
| L | HIS168 | 
| L | HIS173 | 
| L | ALA176 | 
| L | ILE177 | 
| L | SER244 | 
| L | CYS247 | 
| L | MET248 | 
| L | BPH402 | 
| M | TYR210 | 
| M | BCL304 | 
| M | BCL305 | 
| site_id | AC5 | 
| Number of Residues | 21 | 
| Details | BINDING SITE FOR RESIDUE BPH L 402 | 
| Chain | Residue | 
| L | ALA42 | 
| L | ILE49 | 
| L | ALA93 | 
| L | ALA96 | 
| L | PHE97 | 
| L | TRP100 | 
| L | GLU104 | 
| L | ILE117 | 
| L | ALA120 | 
| L | PHE121 | 
| L | ALA124 | 
| L | TYR148 | 
| L | LEU238 | 
| L | VAL241 | 
| L | BCL302 | 
| M | TYR210 | 
| M | ALA213 | 
| M | LEU214 | 
| M | MET218 | 
| M | TRP252 | 
| M | BCL305 | 
| site_id | AC6 | 
| Number of Residues | 12 | 
| Details | BINDING SITE FOR RESIDUE U10 L 502 | 
| Chain | Residue | 
| L | ILE175 | 
| L | THR178 | 
| L | PHE179 | 
| L | LEU189 | 
| L | HIS190 | 
| L | LEU193 | 
| L | PHE216 | 
| L | SER223 | 
| L | ILE224 | 
| L | GLY225 | 
| L | THR226 | 
| L | ILE229 | 
| site_id | AC7 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE DIO L 900 | 
| Chain | Residue | 
| L | TRP263 | 
| L | TRP266 | 
| M | PHE90 | 
| M | HOH313 | 
| site_id | AC8 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE DIO L 901 | 
| Chain | Residue | 
| L | SER239 | 
| site_id | AC9 | 
| Number of Residues | 16 | 
| Details | BINDING SITE FOR RESIDUE BCL M 303 | 
| Chain | Residue | 
| L | HIS168 | 
| L | MET174 | 
| L | THR178 | 
| L | PHE181 | 
| L | THR182 | 
| L | HOH282 | 
| M | LEU89 | 
| M | MET122 | 
| M | LEU160 | 
| M | ILE179 | 
| M | HIS182 | 
| M | LEU183 | 
| M | THR186 | 
| M | BCL304 | 
| M | BPH401 | 
| M | SPN600 | 
| site_id | BC1 | 
| Number of Residues | 24 | 
| Details | BINDING SITE FOR RESIDUE BCL M 304 | 
| Chain | Residue | 
| M | ASN187 | 
| M | PHE189 | 
| M | SER190 | 
| M | LEU196 | 
| M | PHE197 | 
| M | HIS202 | 
| M | SER205 | 
| M | ILE206 | 
| M | TYR210 | 
| M | VAL276 | 
| M | GLY280 | 
| M | ILE284 | 
| M | BCL303 | 
| M | BPH401 | 
| L | VAL157 | 
| L | TYR162 | 
| L | HIS168 | 
| L | PHE181 | 
| L | BCL302 | 
| M | ALA153 | 
| M | LEU156 | 
| M | TRP157 | 
| M | LEU160 | 
| M | THR186 | 
| site_id | BC2 | 
| Number of Residues | 14 | 
| Details | BINDING SITE FOR RESIDUE BCL M 305 | 
| Chain | Residue | 
| L | ILE46 | 
| L | TYR128 | 
| L | HIS153 | 
| L | LEU154 | 
| L | BCL302 | 
| L | BPH402 | 
| M | GLY203 | 
| M | ILE206 | 
| M | ALA207 | 
| M | TYR210 | 
| M | GLY211 | 
| M | LEU214 | 
| M | HOH328 | 
| M | LDA701 | 
| site_id | BC3 | 
| Number of Residues | 16 | 
| Details | BINDING SITE FOR RESIDUE BPH M 401 | 
| Chain | Residue | 
| L | PHE181 | 
| L | LEU185 | 
| L | LEU189 | 
| L | LEU219 | 
| L | VAL220 | 
| M | LEU60 | 
| M | GLY63 | 
| M | PHE67 | 
| M | VAL126 | 
| M | TRP129 | 
| M | THR146 | 
| M | PHE150 | 
| M | ALA153 | 
| M | THR277 | 
| M | BCL303 | 
| M | BCL304 | 
| site_id | BC4 | 
| 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 | BC5 | 
| Number of Residues | 14 | 
| Details | BINDING SITE FOR RESIDUE U10 M 501 | 
| Chain | Residue | 
| H | LDA702 | 
| L | GLY35 | 
| L | TRP100 | 
| M | HIS219 | 
| M | THR222 | 
| M | ALA248 | 
| M | ALA249 | 
| M | TRP252 | 
| M | MET256 | 
| M | PHE258 | 
| M | ASN259 | 
| M | ALA260 | 
| M | ILE265 | 
| M | TRP268 | 
| site_id | BC6 | 
| Number of Residues | 15 | 
| Details | BINDING SITE FOR RESIDUE SPN M 600 | 
| Chain | Residue | 
| M | PHE67 | 
| M | PHE68 | 
| M | ILE70 | 
| M | GLY71 | 
| M | TRP75 | 
| M | PHE105 | 
| M | SER119 | 
| M | TRP157 | 
| M | LEU160 | 
| M | GLY161 | 
| M | TRP171 | 
| M | VAL175 | 
| M | GLY178 | 
| M | HIS182 | 
| M | BCL303 | 
| site_id | BC7 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE LDA M 701 | 
| Chain | Residue | 
| H | LDA702 | 
| M | BCL305 | 
| site_id | BC8 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE LDA M 703 | 
| Chain | Residue | 
| H | LDA704 | 
| M | TRP148 | 
| M | LEU278 | 
| M | PO4800 | 
| M | PO4801 | 
| site_id | BC9 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE LDA M 705 | 
| Chain | Residue | 
| M | TRP41 | 
| M | PHE42 | 
| site_id | CC1 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE LDA M 707 | 
| Chain | Residue | 
| H | LDA702 | 
| M | MET256 | 
| M | GLY257 | 
| site_id | CC2 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE LDA M 708 | 
| Chain | Residue | 
| L | VAL220 | 
| M | GLY31 | 
| site_id | CC3 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE PO4 M 800 | 
| Chain | Residue | 
| H | LDA704 | 
| L | ASN199 | 
| M | HIS145 | 
| M | ARG267 | 
| M | HOH332 | 
| M | LDA703 | 
| site_id | CC4 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE PO4 M 801 | 
| Chain | Residue | 
| M | LYS144 | 
| M | LDA703 | 
| site_id | CC5 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE PO4 M 803 | 
| Chain | Residue | 
| M | ASN28 | 
| M | GLY53 | 
| M | SER54 | 
| M | HOH334 | 
| site_id | CC6 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE DIO M 902 | 
| Chain | Residue | 
| L | PHE119 | 
| M | GLN4 | 
| site_id | CC7 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE CL M 306 | 
| Chain | Residue | 
| M | ILE6 | 
Functional Information from PROSITE/UniProt
| site_id | PS00244 | 
| Number of Residues | 27 | 
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NfhynPaHmiAitffftnalalAlHGA | 
| Chain | Residue | Details | 
| L | ASN166-ALA192 | |
| M | ASN195-ALA221 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 278 | 
| Details | Transmembrane: {"description":"Helical"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 58 | 
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} | 
| 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 | 











