1RVJ
PHOTOSYNTHETIC REACTION CENTER DOUBLE MUTANT FROM RHODOBACTER SPHAEROIDES WITH ASP L213 REPLACED WITH ASN AND ARG H177 REPLACED WITH HIS
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 |
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 | 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BCL L 851 |
Chain | Residue |
L | HIS168 |
M | HIS182 |
M | LEU183 |
M | THR186 |
M | BCL853 |
M | BPH855 |
M | SPO860 |
L | MET174 |
L | ILE177 |
L | SER178 |
L | THR182 |
L | BCL852 |
L | HOH1056 |
M | TRP157 |
M | ILE179 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BCL L 852 |
Chain | Residue |
L | PHE97 |
L | ALA127 |
L | VAL157 |
L | THR160 |
L | TYR162 |
L | ASN166 |
L | PHE167 |
L | HIS168 |
L | HIS173 |
L | ILE177 |
L | PHE180 |
L | SER244 |
L | CYS247 |
L | MET248 |
L | BCL851 |
L | BPH856 |
M | TYR210 |
M | BCL853 |
M | BCL854 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BPH L 856 |
Chain | Residue |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | ILE117 |
L | ALA120 |
L | PHE121 |
L | PHE123 |
L | ALA124 |
L | TYR128 |
L | HIS153 |
L | VAL241 |
L | BCL852 |
M | TYR210 |
M | ALA213 |
M | LEU214 |
M | TRP252 |
M | MET256 |
M | BCL854 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE U10 L 859 |
Chain | Residue |
L | LEU189 |
L | PHE216 |
L | VAL220 |
L | GLY221 |
L | TYR222 |
L | SER223 |
L | ILE224 |
L | ILE229 |
M | SER30 |
M | GLY31 |
M | VAL32 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 M 857 |
Chain | Residue |
L | HIS190 |
L | HIS230 |
M | HIS219 |
M | GLU234 |
M | HIS266 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 M 864 |
Chain | Residue |
M | ASN28 |
M | GLY53 |
M | SER54 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE BCL M 853 |
Chain | Residue |
L | TYR162 |
L | PHE181 |
L | BCL851 |
L | BCL852 |
M | MET122 |
M | ALA153 |
M | LEU156 |
M | TRP157 |
M | LEU160 |
M | THR186 |
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 | BPH855 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BCL M 854 |
Chain | Residue |
L | BCL852 |
L | BPH856 |
M | PHE197 |
M | GLY203 |
M | ILE206 |
M | ALA207 |
M | TYR210 |
M | LEU214 |
M | U10858 |
M | LDA861 |
M | HOH1060 |
L | TYR128 |
L | LEU131 |
L | PHE146 |
L | HIS153 |
L | LEU154 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BPH M 855 |
Chain | Residue |
L | PHE181 |
L | ALA184 |
L | LEU185 |
L | LEU189 |
L | LEU219 |
L | BCL851 |
M | LEU60 |
M | GLY63 |
M | PHE67 |
M | ALA125 |
M | VAL126 |
M | TRP129 |
M | THR146 |
M | ALA149 |
M | PHE150 |
M | ALA273 |
M | VAL274 |
M | THR277 |
M | BCL853 |
site_id | BC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE U10 M 858 |
Chain | Residue |
H | LDA862 |
L | PHE29 |
L | GLY35 |
L | THR38 |
L | TRP100 |
L | ARG103 |
M | HIS219 |
M | THR222 |
M | ALA248 |
M | ALA249 |
M | TRP252 |
M | MET256 |
M | ASN259 |
M | ALA260 |
M | THR261 |
M | TRP268 |
M | BCL854 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SPO M 860 |
Chain | Residue |
L | BCL851 |
M | PHE67 |
M | PHE68 |
M | ILE70 |
M | GLY71 |
M | TRP75 |
M | PHE85 |
M | TRP115 |
M | SER119 |
M | MET122 |
M | TRP157 |
M | LEU160 |
M | GLY161 |
M | PHE162 |
M | TRP171 |
M | GLY178 |
M | HIS182 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LDA M 861 |
Chain | Residue |
H | TRP21 |
H | LDA862 |
M | PHE208 |
M | BCL854 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA M 863 |
Chain | Residue |
H | LDA862 |
L | PRO28 |
M | GLY257 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CDL M 900 |
Chain | Residue |
H | PHE23 |
H | TYR30 |
L | ASN199 |
L | PRO200 |
M | LYS144 |
M | HIS145 |
M | TRP148 |
M | ARG267 |
M | TRP271 |
M | LEU278 |
M | ILE282 |
M | HOH1006 |
M | HOH1054 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA H 862 |
Chain | Residue |
H | TYR40 |
M | PHE258 |
M | U10858 |
M | LDA861 |
M | LDA863 |
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 | 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 |
H | GLN32-ALA260 | |
M | LEU235 | |
M | ARG253 | |
M | ARG267 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
L | LEU154 | |
L | MET174 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
L | GLY191 | |
L | ARG217 | |
L | ARG231 |