1L9J
X-Ray Structure of the Cytochrome-c(2)-Photosynthetic Reaction Center Electron Transfer Complex from Rhodobacter sphaeroides in Type I Co-Crystals
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0042597 | cellular_component | periplasmic space |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0042597 | cellular_component | periplasmic space |
| H | 0019684 | biological_process | photosynthesis, light reaction |
| H | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| H | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| L | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| L | 0019684 | biological_process | photosynthesis, light reaction |
| L | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| L | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| M | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| M | 0019684 | biological_process | photosynthesis, light reaction |
| M | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| M | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| R | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| R | 0019684 | biological_process | photosynthesis, light reaction |
| R | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| R | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| S | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| S | 0019684 | biological_process | photosynthesis, light reaction |
| S | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| S | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| T | 0019684 | biological_process | photosynthesis, light reaction |
| T | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| T | 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 M 1007 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS219 |
| M | GLU234 |
| M | HIS266 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 S 2007 |
| Chain | Residue |
| S | HIS266 |
| R | HIS190 |
| R | HIS230 |
| S | HIS219 |
| S | GLU234 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL S 2012 |
| Chain | Residue |
| S | HIS145 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BCL M 1001 |
| Chain | Residue |
| L | HIS168 |
| L | MET174 |
| L | ILE177 |
| L | SER178 |
| L | PHE181 |
| L | THR182 |
| L | BCL1002 |
| L | BPH1005 |
| M | TRP157 |
| M | HIS182 |
| M | LEU183 |
| M | THR186 |
| M | BCL1003 |
| M | LDA1011 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BCL L 1002 |
| Chain | Residue |
| L | PHE97 |
| L | ALA124 |
| L | TYR128 |
| L | LEU131 |
| L | VAL157 |
| L | TYR162 |
| L | PHE167 |
| L | HIS168 |
| L | HIS173 |
| L | ILE177 |
| L | PHE180 |
| L | SER244 |
| L | ALA245 |
| L | CYS247 |
| L | MET248 |
| L | BCL1004 |
| M | TYR210 |
| M | BCL1001 |
| M | BCL1003 |
| M | BPH1006 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE BCL M 1003 |
| Chain | Residue |
| L | TYR162 |
| L | PHE181 |
| L | BCL1002 |
| L | BCL1004 |
| L | BPH1005 |
| M | TRP66 |
| M | ALA153 |
| M | LEU156 |
| M | TRP157 |
| M | THR186 |
| M | ASN187 |
| M | SER190 |
| M | LEU196 |
| M | PHE197 |
| M | HIS202 |
| M | SER205 |
| M | ILE206 |
| M | TYR210 |
| M | GLY280 |
| M | GLY281 |
| M | ILE284 |
| M | BCL1001 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BCL L 1004 |
| Chain | Residue |
| L | ILE46 |
| L | ILE49 |
| L | TYR128 |
| L | LEU131 |
| L | ILE150 |
| L | TRP151 |
| L | HIS153 |
| L | LEU154 |
| L | BCL1002 |
| M | PHE197 |
| M | GLY203 |
| M | ILE206 |
| M | ALA207 |
| M | TYR210 |
| M | LEU214 |
| M | BCL1003 |
| M | BPH1006 |
| M | LDA1010 |
| M | HOH1025 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BPH L 1005 |
| Chain | Residue |
| M | BCL1001 |
| M | BCL1003 |
| L | PHE181 |
| L | ALA184 |
| L | LEU185 |
| L | LEU189 |
| L | LEU219 |
| M | GLY63 |
| M | TRP129 |
| M | THR146 |
| M | ALA149 |
| M | PHE150 |
| M | ALA153 |
| M | ALA273 |
| M | THR277 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BPH M 1006 |
| Chain | Residue |
| L | ILE46 |
| L | ALA93 |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | PHE121 |
| L | TYR148 |
| L | HIS153 |
| L | LEU238 |
| L | VAL241 |
| L | BCL1002 |
| L | BCL1004 |
| M | TYR210 |
| M | ALA213 |
| M | LEU214 |
| M | MET218 |
| M | TRP252 |
| M | MET256 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE U10 M 1008 |
| Chain | Residue |
| L | TRP100 |
| M | MET218 |
| M | HIS219 |
| M | THR222 |
| M | ILE223 |
| M | ALA249 |
| M | TRP252 |
| M | MET256 |
| M | ASN259 |
| M | ALA260 |
| M | THR261 |
| M | MET262 |
| M | ILE265 |
| M | TRP268 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 1009 |
| Chain | Residue |
| C | CYS15 |
| C | CYS18 |
| C | HIS19 |
| C | PRO38 |
| C | ARG46 |
| C | ALA48 |
| C | GLY49 |
| C | PHE54 |
| C | TYR57 |
| C | GLY58 |
| C | MET61 |
| C | TRP71 |
| C | PHE76 |
| C | TYR79 |
| C | VAL80 |
| C | LYS99 |
| C | MET100 |
| C | THR101 |
| C | PHE102 |
| M | LEU191 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA M 1010 |
| Chain | Residue |
| L | BCL1004 |
| M | LEU204 |
| M | MET272 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LDA M 1011 |
| Chain | Residue |
| M | PHE67 |
| M | PHE74 |
| M | MET122 |
| M | TRP157 |
| M | VAL175 |
| M | PRO176 |
| M | GLY178 |
| M | HIS182 |
| M | BCL1001 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCL S 2001 |
| Chain | Residue |
| R | HIS168 |
| R | MET174 |
| R | ILE177 |
| R | SER178 |
| R | THR182 |
| S | ILE179 |
| S | HIS182 |
| S | LEU183 |
| S | THR186 |
| S | BCL2003 |
| S | LDA2011 |
| site_id | BC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BCL R 2002 |
| Chain | Residue |
| R | PHE97 |
| R | ALA124 |
| R | TYR128 |
| R | LEU131 |
| R | VAL157 |
| R | TYR162 |
| R | PHE167 |
| R | HIS168 |
| R | HIS173 |
| R | ILE177 |
| R | PHE180 |
| R | SER244 |
| R | ALA245 |
| R | CYS247 |
| R | MET248 |
| R | BCL2004 |
| S | BCL2003 |
| S | BPH2006 |
| site_id | BC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE BCL S 2003 |
| Chain | Residue |
| R | VAL157 |
| R | TYR162 |
| R | PHE181 |
| R | BCL2002 |
| R | BPH2005 |
| S | TRP66 |
| S | ALA153 |
| S | LEU156 |
| S | TRP157 |
| S | ASN187 |
| S | PHE189 |
| S | SER190 |
| S | LEU196 |
| S | PHE197 |
| S | HIS202 |
| S | SER205 |
| S | ILE206 |
| S | LEU209 |
| S | TYR210 |
| S | GLY280 |
| S | ILE284 |
| S | BCL2001 |
| site_id | BC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BCL R 2004 |
| Chain | Residue |
| R | ILE46 |
| R | ILE49 |
| R | TYR128 |
| R | LEU131 |
| R | PHE146 |
| R | ILE150 |
| R | TRP151 |
| R | HIS153 |
| R | LEU154 |
| R | BCL2002 |
| S | PHE197 |
| S | GLY203 |
| S | ILE206 |
| S | ALA207 |
| S | TYR210 |
| S | LEU214 |
| S | BPH2006 |
| S | LDA2010 |
| site_id | BC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BPH R 2005 |
| Chain | Residue |
| R | PHE181 |
| R | ALA184 |
| R | LEU185 |
| R | LEU189 |
| R | LEU219 |
| S | SER59 |
| S | LEU60 |
| S | GLY63 |
| S | LEU64 |
| S | ALA125 |
| S | TRP129 |
| S | ALA149 |
| S | PHE150 |
| S | ALA153 |
| S | ALA273 |
| S | BCL2003 |
| site_id | CC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE BPH S 2006 |
| Chain | Residue |
| R | ALA42 |
| R | ILE49 |
| R | ALA93 |
| R | ALA96 |
| R | PHE97 |
| R | TRP100 |
| R | GLU104 |
| R | ILE117 |
| R | ALA120 |
| R | PHE121 |
| R | TYR128 |
| R | TYR148 |
| R | LEU238 |
| R | VAL241 |
| R | BCL2002 |
| R | BCL2004 |
| S | TYR210 |
| S | ALA213 |
| S | LEU214 |
| S | MET218 |
| S | TRP252 |
| S | MET256 |
| site_id | CC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE U10 S 2008 |
| Chain | Residue |
| R | TRP100 |
| S | HIS219 |
| S | THR222 |
| S | ALA249 |
| S | TRP252 |
| S | PHE258 |
| S | ASN259 |
| S | ALA260 |
| S | THR261 |
| S | MET262 |
| S | TRP268 |
| site_id | CC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM D 2009 |
| Chain | Residue |
| D | CYS15 |
| D | CYS18 |
| D | HIS19 |
| D | THR36 |
| D | PRO38 |
| D | ARG46 |
| D | ALA48 |
| D | GLY49 |
| D | PHE54 |
| D | TYR57 |
| D | GLY58 |
| D | MET61 |
| D | TRP71 |
| D | PHE76 |
| D | TYR79 |
| D | LYS99 |
| D | MET100 |
| D | THR101 |
| D | PHE102 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LDA S 2010 |
| Chain | Residue |
| R | BCL2004 |
| S | PRO200 |
| S | LEU204 |
| S | PHE208 |
| T | ILE28 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LDA S 2011 |
| Chain | Residue |
| S | PHE74 |
| S | MET122 |
| S | VAL175 |
| S | PRO176 |
| S | GLY178 |
| S | HIS182 |
| S | BCL2001 |
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 | 116 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 556 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 174 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"covalent"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"8827449","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






