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 | 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 | 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 |