2UXK
X-ray high resolution structure of the photosynthetic reaction center from Rb. sphaeroides at pH 10 in the charge-separated state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BCL M 1303 |
| Chain | Residue |
| L | HIS168 |
| M | HIS182 |
| M | LEU183 |
| M | THR186 |
| M | BCL1304 |
| M | BPH1311 |
| M | SPO1313 |
| M | HOH2142 |
| L | MET174 |
| L | ILE177 |
| L | SER178 |
| L | THR182 |
| L | LEU185 |
| L | LDA1285 |
| M | PHE67 |
| M | MET122 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BCL M 1304 |
| Chain | Residue |
| L | VAL157 |
| L | TYR162 |
| L | PHE181 |
| L | BCL1289 |
| M | ALA153 |
| M | TRP157 |
| M | LEU160 |
| M | THR186 |
| M | ASN187 |
| M | SER190 |
| M | LEU196 |
| M | PHE197 |
| M | HIS202 |
| M | SER205 |
| M | ILE206 |
| M | TYR210 |
| M | VAL276 |
| M | GLY280 |
| M | ILE284 |
| M | BCL1303 |
| M | BPH1311 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCL L 1282 |
| Chain | Residue |
| L | TYR128 |
| L | PHE146 |
| L | HIS153 |
| L | LEU154 |
| L | BPH1287 |
| L | BCL1289 |
| L | HOH2126 |
| M | PHE197 |
| M | GLY203 |
| M | ILE206 |
| M | ALA207 |
| M | TYR210 |
| M | LEU214 |
| M | LDA1305 |
| M | U101312 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LDA M 1305 |
| Chain | Residue |
| L | BCL1282 |
| M | PRO200 |
| M | GLY203 |
| M | PHE208 |
| M | LDA1307 |
| M | GOL1315 |
| M | HOH2145 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA M 1306 |
| Chain | Residue |
| M | SER8 |
| M | LEU38 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LDA M 1307 |
| Chain | Residue |
| H | GLN32 |
| H | TYR40 |
| H | PHE56 |
| M | ARG253 |
| M | PHE258 |
| M | LDA1305 |
| M | LDA1308 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA M 1308 |
| Chain | Residue |
| M | GLY257 |
| M | LDA1307 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA L 1283 |
| Chain | Residue |
| H | GOL1254 |
| L | TYR148 |
| M | GOL1315 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA L 1284 |
| Chain | Residue |
| L | VAL220 |
| L | UQ21288 |
| M | SER30 |
| M | GLY31 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA L 1285 |
| Chain | Residue |
| L | ILE175 |
| L | LDA1286 |
| M | BCL1303 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LDA L 1286 |
| Chain | Residue |
| L | LDA1285 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 1310 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS219 |
| M | GLU234 |
| M | HIS266 |
| site_id | BC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BPH M 1311 |
| Chain | Residue |
| M | PHE150 |
| M | ALA153 |
| M | ALA273 |
| M | THR277 |
| M | BCL1303 |
| M | BCL1304 |
| L | PHE181 |
| L | ALA184 |
| L | LEU185 |
| L | LEU189 |
| L | LEU219 |
| M | SER59 |
| M | LEU60 |
| M | LEU64 |
| M | TRP66 |
| M | PHE67 |
| M | VAL126 |
| M | TRP129 |
| M | THR146 |
| site_id | BC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BPH L 1287 |
| Chain | Residue |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | PHE121 |
| L | ALA124 |
| L | TYR148 |
| L | GLY149 |
| L | HIS153 |
| L | VAL241 |
| L | BCL1282 |
| L | BCL1289 |
| M | TYR210 |
| M | ALA213 |
| M | LEU214 |
| M | TRP252 |
| M | MET256 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE U10 M 1312 |
| Chain | Residue |
| L | PHE29 |
| L | TRP100 |
| L | BCL1282 |
| M | MET218 |
| M | HIS219 |
| M | THR222 |
| M | ALA248 |
| M | ALA249 |
| M | TRP252 |
| M | MET256 |
| M | ASN259 |
| M | ALA260 |
| M | ILE265 |
| M | TRP268 |
| M | MET272 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UQ2 L 1288 |
| 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 |
| L | LDA1284 |
| site_id | BC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BCL L 1289 |
| Chain | Residue |
| L | PHE97 |
| L | ALA127 |
| L | LEU131 |
| L | TRP156 |
| L | VAL157 |
| 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 | BPH1287 |
| M | TYR210 |
| M | BCL1304 |
| site_id | BC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SPO M 1313 |
| Chain | Residue |
| M | PHE67 |
| M | ILE70 |
| M | GLY71 |
| M | TRP75 |
| M | SER119 |
| M | PHE120 |
| M | MET122 |
| M | TRP157 |
| M | GLY161 |
| M | PHE162 |
| M | TRP171 |
| M | VAL175 |
| M | GLY178 |
| M | ILE179 |
| M | HIS182 |
| M | BCL1303 |
| site_id | CC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CDL M 1314 |
| Chain | Residue |
| H | TYR30 |
| H | GOL1251 |
| H | HOH2002 |
| L | ASN199 |
| M | GLY143 |
| M | LYS144 |
| M | HIS145 |
| M | TRP148 |
| M | ARG267 |
| M | LEU278 |
| M | HOH2146 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 L 1290 |
| Chain | Residue |
| H | HIS126 |
| L | GLU72 |
| L | LYS82 |
| L | HOH2127 |
| M | THR21 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HTO L 1291 |
| Chain | Residue |
| L | GLN87 |
| L | ILE91 |
| L | THR94 |
| L | TRP142 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 1251 |
| Chain | Residue |
| H | GLU34 |
| H | ARG37 |
| H | LYS62 |
| H | HOH2001 |
| L | ASN199 |
| L | GOL1292 |
| M | ARG267 |
| M | CDL1314 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL L 1292 |
| Chain | Residue |
| H | THR63 |
| H | PHE64 |
| H | GOL1251 |
| L | ALA198 |
| L | ASN199 |
| L | PRO200 |
| site_id | CC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL L 1293 |
| Chain | Residue |
| L | ALA78 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL M 1315 |
| Chain | Residue |
| L | LDA1283 |
| M | LDA1305 |
| site_id | CC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL H 1252 |
| Chain | Residue |
| H | ALA25 |
| site_id | CC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL H 1253 |
| Chain | Residue |
| H | TRP21 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL H 1254 |
| Chain | Residue |
| H | TRP21 |
| L | LDA1283 |
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 | 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 |
