2RCR
STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES
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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 600 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS217 |
| M | GLU232 |
| M | HIS264 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCL M 601 |
| Chain | Residue |
| L | BCL350 |
| M | LEU158 |
| M | VAL173 |
| M | HIS180 |
| M | TRP183 |
| M | THR184 |
| M | BCL400 |
| M | BPH500 |
| L | HIS168 |
| L | MET174 |
| L | ILE177 |
| L | SER178 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BCL L 350 |
| Chain | Residue |
| L | PHE97 |
| L | ALA124 |
| L | ALA127 |
| L | TYR128 |
| L | TRP156 |
| L | VAL157 |
| L | TYR162 |
| L | HIS168 |
| L | HIS173 |
| L | ILE177 |
| L | PHE180 |
| L | VAL241 |
| L | SER244 |
| L | MET248 |
| L | BCL450 |
| L | BPH550 |
| M | TYR208 |
| M | BCL400 |
| M | BCL601 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BCL M 400 |
| Chain | Residue |
| L | PHE181 |
| L | BCL350 |
| L | BCL450 |
| M | ALA151 |
| M | LEU154 |
| M | LEU158 |
| M | THR184 |
| M | PHE187 |
| M | SER188 |
| M | LEU194 |
| M | PHE195 |
| M | HIS200 |
| M | SER203 |
| M | ILE204 |
| M | TYR208 |
| M | THR275 |
| M | GLY278 |
| M | ILE282 |
| M | BPH500 |
| M | BCL601 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCL L 450 |
| Chain | Residue |
| L | TYR128 |
| L | PHE146 |
| L | HIS153 |
| L | BCL350 |
| L | BPH550 |
| M | PHE195 |
| M | ALA205 |
| M | PHE206 |
| M | BCL400 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BPH M 500 |
| Chain | Residue |
| L | PHE181 |
| L | LEU185 |
| L | LEU189 |
| L | UQ800 |
| M | SER58 |
| M | PHE66 |
| M | TRP127 |
| M | THR131 |
| M | THR144 |
| M | ALA147 |
| M | PHE148 |
| M | ALA271 |
| M | BCL400 |
| M | BCL601 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BPH L 550 |
| Chain | Residue |
| L | PHE41 |
| L | ALA42 |
| L | GLY45 |
| L | ILE49 |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | PHE121 |
| L | TYR148 |
| L | ILE150 |
| L | SER237 |
| L | BCL350 |
| L | BCL450 |
| M | TYR208 |
| M | ALA211 |
| M | LEU212 |
| M | MET216 |
| M | TRP250 |
| M | MET254 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UQ M 750 |
| Chain | Residue |
| M | LEU212 |
| M | MET216 |
| M | THR220 |
| M | ILE221 |
| M | ALA243 |
| M | TRP250 |
| M | MET254 |
| M | PHE256 |
| M | ALA258 |
| M | THR259 |
| M | MET260 |
| M | ILE263 |
| M | TRP266 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE UQ L 800 |
| Chain | Residue |
| L | LEU185 |
| L | HIS190 |
| L | LEU193 |
| L | GLU212 |
| L | PHE216 |
| L | VAL220 |
| L | SER223 |
| L | ILE224 |
| L | ILE229 |
| M | TRP127 |
| M | BPH500 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NlfynPfHglSiaflygsallfAmHGA |
| Chain | Residue | Details |
| M | ASN193-ALA219 | |
| L | ASN166-ALA192 |
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 | 57 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Topological domain: {"description":"Periplasmic"} |
| Chain | Residue | Details |






