5M7J
Blastochloris viridis photosynthetic reaction center structure using best crystal approach
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0019684 | biological_process | photosynthesis, light reaction |
| A | 0020037 | molecular_function | heme binding |
| A | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| B | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016168 | molecular_function | chlorophyll binding |
| B | 0019684 | biological_process | photosynthesis, light reaction |
| B | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| B | 0042314 | molecular_function | bacteriochlorophyll binding |
| B | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016168 | molecular_function | chlorophyll binding |
| C | 0019684 | biological_process | photosynthesis, light reaction |
| C | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| C | 0042314 | molecular_function | bacteriochlorophyll binding |
| C | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016168 | molecular_function | chlorophyll binding |
| D | 0019684 | biological_process | photosynthesis, light reaction |
| D | 0030077 | cellular_component | plasma membrane light-harvesting complex |
| D | 0042314 | molecular_function | bacteriochlorophyll binding |
| D | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEC A 401 |
| Chain | Residue |
| A | TYR56 |
| A | ILE77 |
| A | THR78 |
| A | VAL81 |
| A | SER82 |
| A | CYS87 |
| A | CYS90 |
| A | HIS91 |
| A | LEU96 |
| A | TYR104 |
| A | ALA107 |
| A | LYS57 |
| A | ARG108 |
| A | ASN58 |
| A | VAL59 |
| A | LYS60 |
| A | VAL61 |
| A | LEU62 |
| A | PHE70 |
| A | MET74 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue HEC A 402 |
| Chain | Residue |
| A | TYR89 |
| A | TYR102 |
| A | MET110 |
| A | LEU111 |
| A | MET113 |
| A | THR114 |
| A | CYS132 |
| A | CYS135 |
| A | HIS136 |
| A | PRO140 |
| A | LEU141 |
| A | PRO142 |
| A | LEU289 |
| A | ARG293 |
| A | PRO301 |
| A | HEC404 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue HEC A 403 |
| Chain | Residue |
| A | VAL201 |
| A | ARG202 |
| A | VAL203 |
| A | VAL204 |
| A | PHE230 |
| A | MET233 |
| A | MET234 |
| A | ILE236 |
| A | SER237 |
| A | LEU240 |
| A | CYS244 |
| A | CYS247 |
| A | HIS248 |
| A | PHE253 |
| A | GLU254 |
| A | ARG264 |
| A | ALA267 |
| A | TRP268 |
| A | ARG272 |
| C | ILE189 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue HEC A 404 |
| Chain | Residue |
| A | HIS124 |
| A | VAL125 |
| A | THR128 |
| A | GLY129 |
| A | LEU240 |
| A | GLN263 |
| A | ALA267 |
| A | GLY270 |
| A | ILE271 |
| A | MET273 |
| A | VAL274 |
| A | ASP304 |
| A | CYS305 |
| A | CYS308 |
| A | HIS309 |
| A | THR313 |
| A | LYS314 |
| A | PRO315 |
| A | HEC402 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue DGA A 405 |
| Chain | Residue |
| A | CYS1 |
| B | TRP262 |
| B | TRP265 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue BCL B 301 |
| Chain | Residue |
| B | MET174 |
| B | VAL177 |
| B | SER178 |
| B | PHE181 |
| B | MET185 |
| B | BCL302 |
| C | MET120 |
| C | VAL155 |
| C | ILE158 |
| C | HIS180 |
| C | LEU184 |
| C | BCL401 |
| C | BPB402 |
| C | NS5404 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue BCL B 302 |
| Chain | Residue |
| B | HIS168 |
| B | HIS173 |
| B | SER176 |
| B | PHE241 |
| B | GLY244 |
| B | THR248 |
| B | BCL301 |
| B | BCL303 |
| B | BPB304 |
| C | TYR195 |
| C | BCL401 |
| C | MQ7403 |
| B | PHE97 |
| B | PRO124 |
| B | MET127 |
| B | VAL157 |
| B | ASN158 |
| B | PHE160 |
| B | TRP167 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue BCL B 303 |
| Chain | Residue |
| B | ILE49 |
| B | PHE128 |
| B | PHE146 |
| B | ILE150 |
| B | HIS153 |
| B | LEU154 |
| B | VAL157 |
| B | BCL302 |
| B | BPB304 |
| C | TYR195 |
| C | GLY201 |
| C | ILE204 |
| C | GLY205 |
| C | TYR208 |
| C | BCL401 |
| C | OTP405 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residue BPB B 304 |
| Chain | Residue |
| B | ILE42 |
| B | ILE49 |
| B | TRP100 |
| B | GLU104 |
| B | VAL117 |
| B | PHE121 |
| B | TYR148 |
| B | GLY149 |
| B | ILE150 |
| B | ALA237 |
| B | PHE241 |
| B | BCL302 |
| B | BCL303 |
| C | TYR208 |
| C | LEU212 |
| C | TRP250 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MPG B 305 |
| Chain | Residue |
| B | TRP115 |
| B | HIS116 |
| B | LEU119 |
| B | SER238 |
| C | ALA1 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MPG B 306 |
| Chain | Residue |
| B | PHE179 |
| B | VAL182 |
| B | HIS190 |
| B | PHE216 |
| B | SER223 |
| B | ILE229 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 307 |
| Chain | Residue |
| B | HIS190 |
| B | HIS230 |
| C | HIS217 |
| C | GLU232 |
| C | HIS264 |
| site_id | AD4 |
| Number of Residues | 20 |
| Details | binding site for residue BCL C 401 |
| Chain | Residue |
| B | HIS168 |
| B | PHE181 |
| B | BCL301 |
| B | BCL302 |
| B | BCL303 |
| C | MET120 |
| C | LEU124 |
| C | PHE154 |
| C | VAL155 |
| C | THR185 |
| C | PHE187 |
| C | PHE194 |
| C | TYR195 |
| C | HIS200 |
| C | SER203 |
| C | ILE204 |
| C | TYR208 |
| C | ALA278 |
| C | ILE282 |
| C | BPB402 |
| site_id | AD5 |
| Number of Residues | 17 |
| Details | binding site for residue BPB C 402 |
| Chain | Residue |
| B | PHE181 |
| B | MET185 |
| B | LEU189 |
| B | VAL220 |
| B | BCL301 |
| C | SER63 |
| C | ILE66 |
| C | SER123 |
| C | LEU124 |
| C | TRP127 |
| C | ILE144 |
| C | ASN147 |
| C | PHE148 |
| C | SER271 |
| C | MET275 |
| C | BCL401 |
| C | NS5404 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue MQ7 C 403 |
| Chain | Residue |
| B | TYR29 |
| B | ILE39 |
| B | ARG103 |
| B | BCL302 |
| C | HIS217 |
| C | THR220 |
| C | ALA246 |
| C | TRP250 |
| C | ASN257 |
| C | ALA258 |
| C | VAL263 |
| C | TRP266 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue NS5 C 404 |
| Chain | Residue |
| B | BCL301 |
| C | LEU70 |
| C | GLY117 |
| C | THR121 |
| C | GLY159 |
| C | CYS160 |
| C | GLY176 |
| C | BPB402 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue OTP C 405 |
| Chain | Residue |
| B | PHE62 |
| B | BCL303 |
| C | PRO198 |
| C | GLY201 |
| C | PHE206 |
| D | TRP25 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 C 407 |
| Chain | Residue |
| C | TRP23 |
| C | TYR50 |
| C | GLY52 |
| C | ALA53 |
| C | SER54 |
| C | SER133 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 C 408 |
| Chain | Residue |
| C | HIS143 |
| C | ARG265 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NfyycPwHgfSigfaygcgllfAaHGA |
| Chain | Residue | Details |
| C | ASN193-ALA219 | |
| B | ASN166-GLY192 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Not N-palmitoylated","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1987","firstPage":"2909","lastPage":"2914","volume":"26","journal":"Biochemistry","title":"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein.","authors":["Weyer K.A.","Schaefer W.","Lottspeich F.","Michel H."]}},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-diacylglycerol cysteine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00303","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1987","firstPage":"2909","lastPage":"2914","volume":"26","journal":"Biochemistry","title":"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein.","authors":["Weyer K.A.","Schaefer W.","Lottspeich F.","Michel H."]}},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 147 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 260 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 185 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 7 |
| Details | Binding site: {} |
| Chain | Residue | Details |
