2JIY
PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M149 REPLACED WITH TRP (CHAIN M, AM149W)
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 | 14 |
Details | BINDING SITE FOR RESIDUE BCL L1282 |
Chain | Residue |
L | HIS168 |
M | HIS182 |
M | LEU183 |
M | THR186 |
M | BCL1303 |
M | SPN1309 |
L | MET174 |
L | ILE177 |
L | SER178 |
L | THR182 |
L | BCL1283 |
L | HOH2055 |
M | MET122 |
M | ILE179 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE BCL L1283 |
Chain | Residue |
L | ALA124 |
L | ALA127 |
L | LEU131 |
L | VAL157 |
L | SER158 |
L | TYR162 |
L | ASN166 |
L | PHE167 |
L | HIS168 |
L | HIS173 |
L | ALA176 |
L | ILE177 |
L | PHE180 |
L | SER244 |
L | CYS247 |
L | MET248 |
L | BCL1282 |
L | BCL1284 |
L | BPH1285 |
M | BCL1303 |
M | U101310 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE BCL M1303 |
Chain | Residue |
L | VAL157 |
L | TYR162 |
L | PHE181 |
L | BCL1282 |
L | BCL1283 |
M | TRP66 |
M | ALA153 |
M | LEU156 |
M | LEU160 |
M | THR186 |
M | ASN187 |
M | PHE189 |
M | LEU196 |
M | PHE197 |
M | HIS202 |
M | SER205 |
M | ILE206 |
M | LEU209 |
M | TYR210 |
M | VAL276 |
M | GLY280 |
M | ILE284 |
M | SPN1309 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BCL L1284 |
Chain | Residue |
L | TYR128 |
L | LEU131 |
L | PHE146 |
L | ILE150 |
L | TRP151 |
L | HIS153 |
L | LEU154 |
L | BCL1283 |
L | BPH1285 |
M | PHE197 |
M | GLY203 |
M | ILE206 |
M | ALA207 |
M | TYR210 |
M | LEU214 |
M | LDA1305 |
M | HOH2083 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CDL M1304 |
Chain | Residue |
H | ALA16 |
H | TYR30 |
H | HOH2003 |
L | ASN199 |
L | PRO200 |
M | GLY143 |
M | LYS144 |
M | HIS145 |
M | TRP148 |
M | TRP155 |
M | ARG267 |
M | HOH2121 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE LDA H1251 |
Chain | Residue |
H | GLN32 |
H | TYR40 |
H | GLY54 |
H | HOH2036 |
M | ARG253 |
M | PHE258 |
M | LDA1305 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA M1305 |
Chain | Residue |
H | LDA1251 |
L | BCL1284 |
M | PRO200 |
M | LEU204 |
M | ALA207 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL M1311 |
Chain | Residue |
M | TRP129 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE M1306 |
Chain | Residue |
L | HIS190 |
L | HIS230 |
M | HIS219 |
M | GLU234 |
M | HIS266 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 M1307 |
Chain | Residue |
M | ASN28 |
M | GLY53 |
M | SER54 |
M | HOH2122 |
M | HOH2123 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BPH L1285 |
Chain | Residue |
L | THR38 |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | ILE117 |
L | ALA120 |
L | PHE121 |
L | PHE123 |
L | ALA124 |
L | VAL241 |
L | BCL1283 |
L | BCL1284 |
M | TYR210 |
M | ALA213 |
M | LEU214 |
M | TRP252 |
M | MET256 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE SPN M1309 |
Chain | Residue |
L | BCL1282 |
M | PHE67 |
M | PHE68 |
M | ILE70 |
M | GLY71 |
M | PHE74 |
M | TRP75 |
M | SER119 |
M | TRP157 |
M | GLY161 |
M | TRP171 |
M | HIS182 |
M | BCL1303 |
site_id | BC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE U10 M1310 |
Chain | Residue |
L | PHE29 |
L | TYR30 |
L | BCL1283 |
M | MET218 |
M | HIS219 |
M | THR222 |
M | ALA248 |
M | ALA249 |
M | TRP252 |
M | MET256 |
M | ASN259 |
M | ALA260 |
M | ILE265 |
M | TRP268 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE U10 L1286 |
Chain | Residue |
L | THR182 |
L | LEU189 |
L | HIS190 |
L | LEU193 |
L | GLU212 |
L | ASP213 |
L | PHE216 |
L | TYR222 |
L | SER223 |
L | ILE224 |
L | GLY225 |
L | THR226 |
L | ILE229 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE D12 M1314 |
Chain | Residue |
M | MET256 |
M | GLY257 |
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 | 278 |
Details | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 58 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 87 |
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 |