3DU2
E(L212)A mutant structure of photosynthetic reaction center from Rhodobacter sphaeroides
Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0015979 | biological_process | photosynthesis |
H | 0016020 | cellular_component | membrane |
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 | 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 | 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 | 21 |
Details | BINDING SITE FOR RESIDUE BCL L 502 |
Chain | Residue |
L | PHE97 |
L | PHE167 |
L | HIS168 |
L | HIS173 |
L | ALA176 |
L | ILE177 |
L | SER244 |
L | CYS247 |
L | MET248 |
L | BCL501 |
L | BPH503 |
L | ALA124 |
M | TYR210 |
M | BCL502 |
L | ILE125 |
L | ALA127 |
L | TYR128 |
L | LEU131 |
L | TRP156 |
L | VAL157 |
L | ASN166 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BCL L 501 |
Chain | Residue |
L | TYR128 |
L | PHE146 |
L | ILE150 |
L | HIS153 |
L | LEU154 |
L | BCL502 |
L | BPH503 |
L | HOH1012 |
M | GLY203 |
M | ILE206 |
M | ALA207 |
M | TYR210 |
M | LEU214 |
M | BCL502 |
M | U10504 |
M | LDA701 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BPH L 503 |
Chain | Residue |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | ILE117 |
L | PHE121 |
L | HIS153 |
L | VAL241 |
L | BCL501 |
L | BCL502 |
M | TYR210 |
M | ALA213 |
M | LEU214 |
M | MET218 |
M | TRP252 |
M | MET256 |
M | U10504 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE U10 L 504 |
Chain | Residue |
L | PHE179 |
L | THR182 |
L | LEU193 |
L | PHE216 |
L | TYR222 |
L | SER223 |
L | ILE224 |
L | ILE229 |
L | TRP262 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA L 709 |
Chain | Residue |
L | LEU75 |
L | GLY76 |
L | ILE91 |
L | THR94 |
L | TRP142 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BCL M 501 |
Chain | Residue |
L | HIS168 |
L | MET174 |
L | ILE177 |
L | SER178 |
L | THR182 |
L | LEU185 |
L | HOH1013 |
M | MET122 |
M | ILE179 |
M | HIS182 |
M | LEU183 |
M | THR186 |
M | BCL502 |
M | BPH503 |
M | SPN600 |
site_id | AC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE BCL M 502 |
Chain | Residue |
M | VAL276 |
M | GLY280 |
M | ILE284 |
M | BCL501 |
M | BPH503 |
L | VAL157 |
L | TYR162 |
L | PHE181 |
L | BCL501 |
L | BCL502 |
M | MET122 |
M | LEU156 |
M | LEU160 |
M | THR186 |
M | ASN187 |
M | PHE189 |
M | LEU196 |
M | PHE197 |
M | HIS202 |
M | SER205 |
M | ILE206 |
M | TYR210 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BPH M 503 |
Chain | Residue |
L | PHE181 |
L | LEU189 |
M | LEU64 |
M | TRP129 |
M | THR146 |
M | PHE150 |
M | ALA273 |
M | THR277 |
M | BCL501 |
M | BCL502 |
site_id | AC9 |
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 | BC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE U10 M 504 |
Chain | Residue |
H | LDA703 |
L | TRP100 |
L | BCL501 |
L | BPH503 |
M | MET218 |
M | HIS219 |
M | THR222 |
M | ALA248 |
M | ALA249 |
M | TRP252 |
M | MET256 |
M | ASN259 |
M | ALA260 |
M | MET262 |
M | ILE265 |
M | TRP268 |
M | LDA704 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SPN M 600 |
Chain | Residue |
M | PHE67 |
M | PHE68 |
M | ILE70 |
M | GLY71 |
M | PHE74 |
M | TRP75 |
M | SER119 |
M | TRP157 |
M | GLY161 |
M | TRP171 |
M | VAL175 |
M | GLY178 |
M | HIS182 |
M | BCL501 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CDL M 800 |
Chain | Residue |
H | TYR30 |
L | ASN199 |
L | PRO200 |
M | GLY143 |
M | LYS144 |
M | HIS145 |
M | TRP148 |
M | TRP155 |
M | ARG267 |
M | ILE270 |
M | TRP271 |
M | HOH1083 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA M 701 |
Chain | Residue |
H | LDA703 |
L | BCL501 |
M | PHE208 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA M 704 |
Chain | Residue |
M | MET256 |
M | GLY257 |
M | U10504 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA H 703 |
Chain | Residue |
H | TYR40 |
M | U10504 |
M | LDA701 |
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 | ASN195-ALA221 | |
L | ASN166-ALA192 |
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 | LYS110-ALA139 | |
M | MET142-LEU167 | |
M | PHE197-ALA225 | |
M | ASN259-LEU285 |
site_id | SWS_FT_FI2 |
Number of Residues | 19 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
H | LEU12-LEU31 | |
M | HIS202 | |
L | HIS116-MET138 | |
L | PRO171-ALA198 | |
L | GLY225-ILE250 |
site_id | SWS_FT_FI3 |
Number of Residues | 228 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
H | GLN32-ALA260 | |
M | GLU234 | |
M | TRP252 | |
M | HIS266 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
L | HIS153 | |
L | HIS173 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
L | HIS190 | |
L | PHE216 | |
L | HIS230 |