6Z27
Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV LCP crystallization
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0015979 | biological_process | photosynthesis |
| 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 | 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 | 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 | 6 |
| Details | binding site for residue LDA H 701 |
| Chain | Residue |
| H | TRP21 |
| H | LDA702 |
| M | PRO200 |
| M | ALA207 |
| M | MET272 |
| M | BCL405 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue LDA H 702 |
| Chain | Residue |
| M | ARG253 |
| M | PHE258 |
| H | GLN32 |
| H | TYR40 |
| H | LDA701 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 H 703 |
| Chain | Residue |
| H | HIS128 |
| H | ASN129 |
| H | LYS132 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 H 704 |
| Chain | Residue |
| H | THR90 |
| H | HIS141 |
| H | VAL142 |
| H | ASN147 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 H 705 |
| Chain | Residue |
| H | GLY71 |
| H | THR72 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue OLC L 301 |
| Chain | Residue |
| L | LEU185 |
| L | HIS190 |
| L | LEU193 |
| L | ASP213 |
| L | PHE216 |
| L | SER223 |
| L | ILE224 |
| L | GLY225 |
| L | THR226 |
| L | ILE229 |
| L | HOH436 |
| L | HOH444 |
| M | BCL404 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue LDA L 302 |
| Chain | Residue |
| L | ALA78 |
| L | GLN87 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue BCL L 303 |
| Chain | Residue |
| L | PHE97 |
| L | ALA124 |
| L | ILE125 |
| L | ALA127 |
| L | LEU131 |
| L | TRP156 |
| L | THR160 |
| L | HIS168 |
| L | HIS173 |
| L | ALA176 |
| L | ILE177 |
| L | PHE180 |
| L | SER244 |
| L | CYS247 |
| L | MET248 |
| L | BPH304 |
| M | TYR210 |
| M | BCL403 |
| M | BCL404 |
| M | BCL405 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | binding site for residue BPH L 304 |
| Chain | Residue |
| L | ILE49 |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| L | ALA120 |
| L | PHE121 |
| L | ALA124 |
| L | TYR148 |
| L | GLY149 |
| L | ILE150 |
| L | HIS153 |
| L | VAL241 |
| L | BCL303 |
| M | TYR210 |
| M | ALA213 |
| M | LEU214 |
| M | TRP252 |
| M | MET256 |
| M | BCL405 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue OLC M 401 |
| Chain | Residue |
| M | PHE67 |
| M | GLY71 |
| M | TRP75 |
| M | MET122 |
| M | TRP157 |
| M | GLY161 |
| M | PHE162 |
| M | VAL175 |
| M | TYR177 |
| M | HIS182 |
| M | BCL403 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue LDA M 402 |
| Chain | Residue |
| M | LEU167 |
| M | THR289 |
| M | ASP292 |
| site_id | AD3 |
| Number of Residues | 20 |
| Details | binding site for residue BCL M 403 |
| Chain | Residue |
| M | MET122 |
| M | TRP157 |
| M | ILE179 |
| M | HIS182 |
| M | LEU183 |
| M | THR186 |
| M | OLC401 |
| M | BCL404 |
| M | BPH406 |
| M | HOH532 |
| L | HIS168 |
| L | MET174 |
| L | ILE177 |
| L | THR178 |
| L | PHE181 |
| L | THR182 |
| L | LEU185 |
| L | BCL303 |
| M | TRP66 |
| M | PHE67 |
| site_id | AD4 |
| Number of Residues | 24 |
| Details | binding site for residue BCL M 404 |
| Chain | Residue |
| L | VAL157 |
| L | TYR162 |
| L | HIS168 |
| L | PHE181 |
| L | OLC301 |
| L | BCL303 |
| M | ALA153 |
| M | LEU156 |
| 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 | BCL403 |
| M | BCL405 |
| M | BPH406 |
| site_id | AD5 |
| Number of Residues | 16 |
| Details | binding site for residue BCL M 405 |
| Chain | Residue |
| H | LDA701 |
| L | TYR128 |
| L | PHE146 |
| L | ILE150 |
| L | HIS153 |
| L | LEU154 |
| L | BCL303 |
| L | BPH304 |
| M | PHE197 |
| M | GLY203 |
| M | ILE206 |
| M | ALA207 |
| M | TYR210 |
| M | GLY211 |
| M | BCL404 |
| M | HOH530 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue BPH M 406 |
| Chain | Residue |
| L | PHE181 |
| L | LEU185 |
| L | LEU189 |
| M | SER59 |
| M | LEU60 |
| M | GLY63 |
| M | PHE67 |
| M | TRP129 |
| M | THR146 |
| M | ALA149 |
| M | PHE150 |
| M | ALA153 |
| M | ALA273 |
| M | THR277 |
| M | BCL403 |
| M | BCL404 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue FE M 407 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS219 |
| M | GLU234 |
| M | HIS266 |
| site_id | AD8 |
| Number of Residues | 17 |
| Details | binding site for residue U10 M 408 |
| Chain | Residue |
| L | PHE29 |
| L | GLY35 |
| L | THR38 |
| L | ARG103 |
| M | MET218 |
| M | HIS219 |
| M | THR222 |
| M | ALA248 |
| M | ALA249 |
| M | TRP252 |
| M | MET256 |
| M | PHE258 |
| M | ASN259 |
| M | ALA260 |
| M | THR261 |
| M | ILE265 |
| M | TRP268 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue LDA M 409 |
| Chain | Residue |
| M | PHE7 |
| M | TRP41 |
| M | PHE42 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue LDA M 410 |
| Chain | Residue |
| L | VAL220 |
| M | GLY31 |
| M | VAL32 |
| site_id | AE2 |
| Number of Residues | 1 |
| Details | binding site for residue LDA M 411 |
| Chain | Residue |
| M | GLY257 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 M 412 |
| Chain | Residue |
| L | ASN199 |
| L | LYS202 |
| L | HOH414 |
| M | HIS145 |
| M | ARG267 |
| M | PO4415 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 M 413 |
| Chain | Residue |
| M | ASN25 |
| M | ASN28 |
| M | TYR51 |
| M | GLY53 |
| M | SER54 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 M 414 |
| Chain | Residue |
| M | SER36 |
| M | THR37 |
| M | LEU38 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 M 415 |
| Chain | Residue |
| L | LYS202 |
| M | GLY143 |
| M | LYS144 |
| M | HIS145 |
| M | PO4412 |
| M | HOH503 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 M 416 |
| Chain | Residue |
| M | TYR3 |
| M | GLN4 |
| M | ASN5 |
| M | ILE6 |
| M | PHE7 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO M 417 |
| Chain | Residue |
| H | HIS126 |
| M | MET20 |
| M | THR21 |
| M | GLU22 |
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 | 57 |
| 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 |






