1F6N
CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT REACTION CENTER PRO L209-> TYR FROM THE PHOTOSYNTHETIC PURPLE BACTERIUM RHODOBACTER SPHAEROIDES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016020 | cellular_component | membrane |
| 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 |
| H | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
| L | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| L | 0015979 | biological_process | photosynthesis |
| L | 0016020 | cellular_component | membrane |
| 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 | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
| L | 0046872 | molecular_function | metal ion binding |
| M | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| M | 0015979 | biological_process | photosynthesis |
| M | 0016020 | cellular_component | membrane |
| 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 | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
| 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 500 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS219 |
| M | GLU234 |
| M | HIS266 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 M 800 |
| Chain | Residue |
| L | ASN199 |
| M | HIS145 |
| M | ARG267 |
| M | LDA704 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCL L 301 |
| Chain | Residue |
| L | MET174 |
| L | ILE177 |
| L | SER178 |
| L | THR182 |
| L | BCL302 |
| L | HOH714 |
| M | ILE179 |
| M | HIS182 |
| M | LEU183 |
| M | BPH401 |
| M | SPO600 |
| M | BCL801 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BCL L 302 |
| Chain | Residue |
| L | PHE97 |
| L | ALA124 |
| L | ILE125 |
| L | ALA127 |
| L | TYR128 |
| L | LEU131 |
| L | TRP156 |
| L | PHE167 |
| L | HIS168 |
| L | HIS173 |
| L | ILE177 |
| L | SER244 |
| L | CYS247 |
| L | MET248 |
| L | BCL301 |
| L | BCL304 |
| L | BPH402 |
| M | TYR210 |
| M | BCL801 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BCL M 801 |
| Chain | Residue |
| L | TYR162 |
| L | PHE181 |
| L | BCL301 |
| L | BCL302 |
| L | BCL304 |
| M | MET122 |
| M | ALA153 |
| M | LEU156 |
| M | LEU160 |
| M | THR186 |
| M | ASN187 |
| M | SER190 |
| M | LEU196 |
| M | PHE197 |
| M | HIS202 |
| M | SER205 |
| M | ILE206 |
| M | TYR210 |
| M | GLY280 |
| M | ILE284 |
| M | BPH401 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCL L 304 |
| Chain | Residue |
| L | TYR128 |
| L | ILE150 |
| L | HIS153 |
| L | LEU154 |
| L | BCL302 |
| L | BPH402 |
| M | GLY203 |
| M | ILE206 |
| M | ALA207 |
| M | TYR210 |
| M | LDA701 |
| M | BCL801 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BPH M 401 |
| Chain | Residue |
| L | PHE181 |
| L | ALA184 |
| L | LEU185 |
| L | LEU189 |
| L | BCL301 |
| L | U10502 |
| M | GLY63 |
| M | LEU64 |
| M | PHE67 |
| M | TRP129 |
| M | THR146 |
| M | PHE150 |
| M | ALA153 |
| M | THR277 |
| M | BCL801 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE BPH L 402 |
| Chain | Residue |
| L | ALA124 |
| L | TYR148 |
| L | LEU238 |
| L | VAL241 |
| L | BCL302 |
| L | BCL304 |
| M | TYR210 |
| M | ALA213 |
| M | LEU214 |
| M | TRP252 |
| M | MET256 |
| L | THR38 |
| L | PHE41 |
| L | CYS92 |
| L | ALA93 |
| L | ALA96 |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | ALA120 |
| L | PHE121 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE U10 M 501 |
| Chain | Residue |
| L | PHE29 |
| L | GLY35 |
| L | TRP100 |
| M | HIS219 |
| M | THR222 |
| M | ALA249 |
| M | TRP252 |
| M | MET256 |
| M | ASN259 |
| M | ALA260 |
| M | ILE265 |
| M | TRP268 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE U10 L 502 |
| Chain | Residue |
| L | HIS190 |
| L | LEU193 |
| L | ASP213 |
| L | PHE216 |
| L | VAL220 |
| L | SER223 |
| L | ILE224 |
| L | GLY225 |
| L | THR226 |
| L | ILE229 |
| M | LEU52 |
| M | TRP129 |
| M | BPH401 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SPO M 600 |
| Chain | Residue |
| L | BCL301 |
| M | PHE67 |
| M | ILE70 |
| M | GLY71 |
| M | TRP75 |
| M | SER119 |
| M | TRP157 |
| M | GLY161 |
| M | GLY178 |
| M | ILE179 |
| M | HIS182 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA M 701 |
| Chain | Residue |
| L | BCL304 |
| M | PRO200 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LDA H 702 |
| Chain | Residue |
| H | ILE28 |
| H | GLN32 |
| H | TYR40 |
| H | GLN53 |
| H | PHE56 |
| L | LDA703 |
| M | ARG253 |
| M | PHE258 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA L 703 |
| Chain | Residue |
| H | LDA702 |
| H | HOH744 |
| H | HOH747 |
| L | PRO28 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA M 704 |
| Chain | Residue |
| H | LDA705 |
| M | HIS145 |
| M | TRP271 |
| M | PO4800 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA H 705 |
| Chain | Residue |
| H | PHE23 |
| H | GLY26 |
| H | TYR30 |
| M | LDA704 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NlfynPfHglSiaflygsallfAmHGA |
| Chain | Residue | Details |
| L | ASN166-ALA192 | |
| M | ASN195-ALA221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| H | MET1-ASP11 | |
| M | GLU111-LEU140 | |
| M | GLY143-MET168 | |
| M | TYR198-VAL226 | |
| M | ALA260-LEU286 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| H | LEU12-LEU31 | |
| M | GLY203 | |
| L | ILE117-MET139 | |
| L | ALA172-ASN199 | |
| L | THR226-THR251 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 228 |
| Details | TOPO_DOM: Cytoplasmic |
| Chain | Residue | Details |
| M | ARG267 | |
| H | GLN32-ALA260 | |
| M | LEU235 | |
| M | ARG253 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| L | MET174 | |
| L | LEU154 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| L | ARG231 | |
| L | GLY191 | |
| L | ARG217 |
