4IN6
(M)L214A mutant of the Rhodobacter sphaeroides Reaction Center
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 | 15 |
| Details | BINDING SITE FOR RESIDUE BPH L 301 |
| Chain | Residue |
| L | PHE97 |
| L | BCL308 |
| M | TYR210 |
| M | ALA213 |
| M | ALA214 |
| M | TRP252 |
| M | MET256 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | ALA120 |
| L | PHE121 |
| L | ALA124 |
| L | HIS153 |
| L | VAL241 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE U10 L 302 |
| Chain | Residue |
| L | ALA186 |
| L | LEU189 |
| L | HIS190 |
| L | LEU193 |
| L | GLU212 |
| L | ASP213 |
| L | PHE216 |
| L | TYR222 |
| L | SER223 |
| L | ILE224 |
| L | GLY225 |
| L | THR226 |
| L | ILE229 |
| M | PC1410 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BCL L 303 |
| Chain | Residue |
| L | PHE97 |
| L | ALA124 |
| L | ALA127 |
| L | LEU131 |
| 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 | BCL308 |
| M | TYR210 |
| M | BCL401 |
| M | BCL402 |
| M | U10407 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 L 304 |
| Chain | Residue |
| H | HIS126 |
| L | GLU72 |
| L | TYR73 |
| L | LYS82 |
| M | THR21 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HTO L 305 |
| Chain | Residue |
| L | GLN87 |
| L | TRP142 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL L 306 |
| Chain | Residue |
| H | THR63 |
| H | PHE64 |
| H | HOH426 |
| L | ALA198 |
| L | ASN199 |
| L | PRO200 |
| M | CDL409 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL L 307 |
| Chain | Residue |
| L | ALA78 |
| L | LEU80 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCL L 308 |
| Chain | Residue |
| L | TYR128 |
| L | PHE146 |
| L | ILE150 |
| L | HIS153 |
| L | LEU154 |
| L | BPH301 |
| L | BCL303 |
| L | HOH426 |
| M | PHE197 |
| M | GLY203 |
| M | ILE206 |
| M | ALA207 |
| M | TYR210 |
| M | GLY211 |
| M | LDA403 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL L 309 |
| Chain | Residue |
| H | GOL303 |
| L | GLN62 |
| M | LDA403 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 L 310 |
| Chain | Residue |
| L | LEU44 |
| L | ILE88 |
| L | ILE91 |
| L | CYS92 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL L 311 |
| Chain | Residue |
| L | SER52 |
| L | TYR67 |
| L | LEU80 |
| L | ALA81 |
| L | GLY83 |
| L | HOH425 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL L 312 |
| Chain | Residue |
| L | TYR148 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL L 313 |
| Chain | Residue |
| L | HOH414 |
| L | HOH424 |
| L | HOH428 |
| H | ASP46 |
| H | GLY47 |
| L | SER4 |
| L | ARG7 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCL M 401 |
| Chain | Residue |
| L | HIS168 |
| L | MET174 |
| L | ILE177 |
| L | SER178 |
| L | THR182 |
| L | BCL303 |
| L | HOH403 |
| M | MET122 |
| M | ILE179 |
| M | HIS182 |
| M | LEU183 |
| M | THR186 |
| M | BCL402 |
| M | BPH406 |
| M | SPO408 |
| site_id | BC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BCL M 402 |
| Chain | Residue |
| L | VAL157 |
| L | PHE181 |
| L | BCL303 |
| M | LEU160 |
| M | THR186 |
| M | ASN187 |
| M | PHE189 |
| M | SER190 |
| M | ASN195 |
| M | LEU196 |
| M | PHE197 |
| M | HIS202 |
| M | SER205 |
| M | ILE206 |
| M | TYR210 |
| M | VAL276 |
| M | GLY280 |
| M | ILE284 |
| M | BCL401 |
| M | BPH406 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA M 403 |
| Chain | Residue |
| L | BCL308 |
| L | GOL309 |
| M | PRO200 |
| M | LEU204 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA M 404 |
| Chain | Residue |
| M | LEU38 |
| M | TRP41 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 405 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS219 |
| M | GLU234 |
| M | HIS266 |
| site_id | CC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BPH M 406 |
| Chain | Residue |
| L | PHE181 |
| L | LEU185 |
| L | LEU189 |
| L | LEU219 |
| M | ALA125 |
| M | VAL126 |
| M | TRP129 |
| M | ALA149 |
| M | PHE150 |
| M | ALA273 |
| M | THR277 |
| M | BCL401 |
| M | BCL402 |
| site_id | CC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE U10 M 407 |
| Chain | Residue |
| L | PHE29 |
| L | TRP100 |
| L | BCL303 |
| M | HIS219 |
| M | THR222 |
| M | ALA248 |
| M | ALA249 |
| M | TRP252 |
| M | MET256 |
| M | PHE258 |
| M | ASN259 |
| M | ALA260 |
| M | THR261 |
| M | ILE265 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SPO M 408 |
| Chain | Residue |
| M | PHE67 |
| M | ILE70 |
| M | GLY71 |
| M | TRP75 |
| M | SER119 |
| M | PHE120 |
| M | TRP157 |
| M | GLY161 |
| M | TRP171 |
| M | VAL175 |
| M | ILE179 |
| M | HIS182 |
| M | BCL401 |
| site_id | CC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDL M 409 |
| Chain | Residue |
| H | ALA16 |
| H | TYR30 |
| H | HOH418 |
| L | ASN199 |
| L | PRO200 |
| L | GOL306 |
| M | GLY143 |
| M | LYS144 |
| M | HIS145 |
| M | TRP148 |
| M | ARG267 |
| M | HOH502 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PC1 M 410 |
| Chain | Residue |
| L | VAL220 |
| L | U10302 |
| M | ALA27 |
| M | SER30 |
| M | GLY31 |
| M | VAL32 |
| M | LEU52 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 M 411 |
| Chain | Residue |
| M | ASN28 |
| M | GLY53 |
| M | SER54 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 M 412 |
| Chain | Residue |
| H | MET175 |
| H | ALA176 |
| L | ARG231 |
| M | TYR3 |
| M | ASN5 |
| M | SER8 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA M 413 |
| Chain | Residue |
| M | LEU167 |
| M | MET168 |
| M | LEU285 |
| M | THR289 |
| site_id | CC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GGD H 301 |
| Chain | Residue |
| H | GLN32 |
| H | TYR40 |
| H | ASN52 |
| H | GLY54 |
| H | PHE56 |
| H | GOL302 |
| M | ARG253 |
| M | MET256 |
| M | GLY257 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL H 302 |
| Chain | Residue |
| H | TRP21 |
| H | ALA25 |
| H | ILE28 |
| H | GGD301 |
| site_id | DC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL H 303 |
| Chain | Residue |
| H | TRP21 |
| L | GOL309 |
| site_id | DC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 H 304 |
| Chain | Residue |
| H | MET134 |
| H | LYS135 |
| H | ALA136 |
| H | ALA137 |
| H | ALA138 |
| H | GLY139 |
| H | PHE140 |
| H | GOL307 |
| H | HOH430 |
| M | TYR295 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL H 305 |
| Chain | Residue |
| H | HIS128 |
| H | ASN129 |
| H | LYS132 |
| site_id | DC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL H 306 |
| Chain | Residue |
| H | ARG177 |
| H | PHE178 |
| H | GLN194 |
| H | GLU230 |
| H | CYS234 |
| M | SER227 |
| M | ARG228 |
| M | GLY230 |
| M | ARG233 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL H 307 |
| Chain | Residue |
| H | ALA138 |
| H | GLY139 |
| H | PHE140 |
| H | PO4304 |
| H | HOH430 |
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 => ECO:0000250 |
| 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 => ECO:0000250 |
| 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 => ECO:0000250 |
| 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 => ECO:0000250 |
| Chain | Residue | Details |
| L | HIS153 | |
| L | HIS173 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| L | HIS190 | |
| L | PHE216 | |
| L | HIS230 |
