6ZI4
Ultrafast Structural Response to Charge Redistribution Within a Photosynthetic Reaction Centre - 5 ps (a) structure
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| C | 0005506 | molecular_function | iron ion binding | 
| C | 0009055 | molecular_function | electron transfer activity | 
| C | 0015979 | biological_process | photosynthesis | 
| C | 0019684 | biological_process | photosynthesis, light reaction | 
| C | 0020037 | molecular_function | heme binding | 
| C | 0030077 | cellular_component | plasma membrane light-harvesting complex | 
| C | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane | 
| C | 0046872 | molecular_function | metal ion binding | 
| 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 | 21 | 
| Details | binding site for residue HEC C 401 | 
| Chain | Residue | 
| C | TYR56 | 
| C | THR75 | 
| C | ILE77 | 
| C | THR78 | 
| C | SER82 | 
| C | CYS87 | 
| C | CYS90 | 
| C | HIS91 | 
| C | ALA97 | 
| C | TYR104 | 
| C | ALA107 | 
| C | LYS57 | 
| C | ARG108 | 
| C | VAL212 | 
| C | ASN58 | 
| C | VAL59 | 
| C | LYS60 | 
| C | VAL61 | 
| C | LEU62 | 
| C | PHE70 | 
| C | MET74 | 
| site_id | AC2 | 
| Number of Residues | 19 | 
| Details | binding site for residue HEC C 402 | 
| Chain | Residue | 
| C | ILE77 | 
| C | VAL81 | 
| C | TYR89 | 
| C | TYR102 | 
| C | PRO103 | 
| C | VAL106 | 
| C | MET110 | 
| C | LEU111 | 
| C | MET113 | 
| C | THR114 | 
| C | THR131 | 
| C | CYS132 | 
| C | CYS135 | 
| C | HIS136 | 
| C | PRO140 | 
| C | LEU141 | 
| C | PRO142 | 
| C | LEU289 | 
| C | ARG293 | 
| site_id | AC3 | 
| Number of Residues | 20 | 
| Details | binding site for residue HEC C 403 | 
| Chain | Residue | 
| C | VAL201 | 
| C | ARG202 | 
| C | VAL203 | 
| C | VAL204 | 
| C | MET233 | 
| C | SER237 | 
| C | LEU240 | 
| C | ASN243 | 
| C | CYS244 | 
| C | CYS247 | 
| C | HIS248 | 
| C | PHE253 | 
| C | GLU254 | 
| C | ARG264 | 
| C | ALA267 | 
| C | TRP268 | 
| C | ARG272 | 
| C | HEC404 | 
| L | TYR162 | 
| M | ILE189 | 
| site_id | AC4 | 
| Number of Residues | 18 | 
| Details | binding site for residue HEC C 404 | 
| Chain | Residue | 
| C | HIS124 | 
| C | THR128 | 
| C | GLY129 | 
| C | ILE236 | 
| C | GLN263 | 
| C | ILE266 | 
| C | GLY270 | 
| C | ILE271 | 
| C | MET273 | 
| C | VAL274 | 
| C | ASP304 | 
| C | CYS305 | 
| C | CYS308 | 
| C | HIS309 | 
| C | THR313 | 
| C | LYS314 | 
| C | PRO315 | 
| C | HEC403 | 
| site_id | AC5 | 
| Number of Residues | 2 | 
| Details | binding site for residue DGA C 405 | 
| Chain | Residue | 
| C | CYS1 | 
| L | TRP265 | 
| site_id | AC6 | 
| Number of Residues | 3 | 
| Details | binding site for residue SO4 C 406 | 
| Chain | Residue | 
| C | THR168 | 
| C | ARG169 | 
| C | SER170 | 
| site_id | AC7 | 
| Number of Residues | 5 | 
| Details | binding site for residue LDA H 701 | 
| Chain | Residue | 
| H | ARG33 | 
| H | PRO54 | 
| H | ASP56 | 
| L | LDA305 | 
| M | PHE256 | 
| site_id | AC8 | 
| Number of Residues | 6 | 
| Details | binding site for residue SO4 H 702 | 
| Chain | Residue | 
| H | ARG33 | 
| H | ARG37 | 
| H | TYR41 | 
| H | GLU61 | 
| H | HOH801 | 
| M | ARG251 | 
| site_id | AC9 | 
| Number of Residues | 3 | 
| Details | binding site for residue SO4 H 703 | 
| Chain | Residue | 
| H | TYR117 | 
| H | ARG233 | 
| H | LYS237 | 
| site_id | AD1 | 
| Number of Residues | 3 | 
| Details | binding site for residue SO4 H 704 | 
| Chain | Residue | 
| H | VAL59 | 
| H | TRP25 | 
| H | THR26 | 
| site_id | AD2 | 
| Number of Residues | 4 | 
| Details | binding site for residue SO4 H 705 | 
| Chain | Residue | 
| H | ARG34 | 
| H | ARG34 | 
| H | LDA707 | 
| H | LDA707 | 
| site_id | AD3 | 
| Number of Residues | 6 | 
| Details | binding site for residue LDA H 706 | 
| Chain | Residue | 
| H | GLN14 | 
| H | TYR18 | 
| L | BCB302 | 
| M | TYR195 | 
| M | HIS299 | 
| M | ALA301 | 
| site_id | AD4 | 
| Number of Residues | 7 | 
| Details | binding site for residue LDA H 707 | 
| Chain | Residue | 
| H | PRO42 | 
| H | VAL59 | 
| H | TYR60 | 
| H | LEU62 | 
| H | TYR64 | 
| H | SO4705 | 
| H | SO4705 | 
| site_id | AD5 | 
| Number of Residues | 4 | 
| Details | binding site for residue HTO H 708 | 
| Chain | Residue | 
| C | ARG216 | 
| H | HIS3 | 
| H | GLY4 | 
| H | ALA5 | 
| site_id | AD6 | 
| Number of Residues | 24 | 
| Details | binding site for residue BCB L 301 | 
| Chain | Residue | 
| L | PHE97 | 
| L | MET127 | 
| L | PHE128 | 
| L | LEU131 | 
| L | VAL157 | 
| L | ASN158 | 
| L | PHE160 | 
| L | TYR162 | 
| L | TRP167 | 
| L | HIS168 | 
| L | HIS173 | 
| L | SER176 | 
| L | VAL177 | 
| L | LEU180 | 
| L | PHE241 | 
| L | GLY244 | 
| L | THR248 | 
| L | BCB302 | 
| L | BPB303 | 
| L | BCB304 | 
| M | TYR195 | 
| M | TYR208 | 
| M | MQ7402 | 
| M | BCB403 | 
| site_id | AD7 | 
| Number of Residues | 17 | 
| Details | binding site for residue BCB L 302 | 
| Chain | Residue | 
| H | LDA706 | 
| L | PHE128 | 
| L | PHE146 | 
| L | ILE150 | 
| L | HIS153 | 
| L | LEU154 | 
| L | VAL157 | 
| L | BCB301 | 
| L | BPB303 | 
| M | TYR195 | 
| M | GLY201 | 
| M | ILE204 | 
| M | GLY205 | 
| M | TYR208 | 
| M | GLY209 | 
| M | MQ7402 | 
| M | BCB403 | 
| site_id | AD8 | 
| Number of Residues | 21 | 
| Details | binding site for residue BPB L 303 | 
| Chain | Residue | 
| L | ILE42 | 
| L | PHE97 | 
| L | TRP100 | 
| L | GLU104 | 
| L | VAL117 | 
| L | ALA120 | 
| L | PHE121 | 
| L | VAL123 | 
| L | PRO124 | 
| L | TYR148 | 
| L | GLY149 | 
| L | ALA237 | 
| L | PHE241 | 
| L | BCB301 | 
| L | BCB302 | 
| M | TYR208 | 
| M | GLY211 | 
| M | LEU212 | 
| M | TRP250 | 
| M | ILE254 | 
| M | MQ7402 | 
| site_id | AD9 | 
| Number of Residues | 16 | 
| Details | binding site for residue BCB L 304 | 
| Chain | Residue | 
| L | HIS168 | 
| L | MET174 | 
| L | VAL177 | 
| L | SER178 | 
| L | PHE181 | 
| L | VAL182 | 
| L | MET185 | 
| L | BCB301 | 
| M | VAL155 | 
| M | TRP178 | 
| M | HIS180 | 
| M | ILE181 | 
| M | LEU184 | 
| M | BCB403 | 
| M | BPB404 | 
| M | NS5405 | 
| site_id | AE1 | 
| Number of Residues | 6 | 
| Details | binding site for residue LDA L 305 | 
| Chain | Residue | 
| H | LEU52 | 
| H | ALA53 | 
| H | LDA701 | 
| L | TYR29 | 
| M | ILE254 | 
| M | PHE256 | 
| site_id | AE2 | 
| Number of Residues | 3 | 
| Details | binding site for residue HTO L 306 | 
| Chain | Residue | 
| L | LEU75 | 
| L | GLN87 | 
| L | TRP142 | 
| site_id | AE3 | 
| Number of Residues | 5 | 
| Details | binding site for residue FE M 401 | 
| Chain | Residue | 
| L | HIS190 | 
| L | HIS230 | 
| M | HIS217 | 
| M | GLU232 | 
| M | HIS264 | 
| site_id | AE4 | 
| Number of Residues | 19 | 
| Details | binding site for residue MQ7 M 402 | 
| Chain | Residue | 
| L | TYR29 | 
| L | GLY35 | 
| L | TRP100 | 
| L | BCB301 | 
| L | BCB302 | 
| L | BPB303 | 
| M | LEU212 | 
| M | ALA216 | 
| M | HIS217 | 
| M | THR220 | 
| M | ALA246 | 
| M | ALA247 | 
| M | TRP250 | 
| M | ILE254 | 
| M | ASN257 | 
| M | ALA258 | 
| M | ILE260 | 
| M | VAL263 | 
| M | TRP266 | 
| site_id | AE5 | 
| Number of Residues | 24 | 
| Details | binding site for residue BCB M 403 | 
| Chain | Residue | 
| L | VAL157 | 
| L | TYR162 | 
| L | PHE181 | 
| L | BCB301 | 
| L | BCB302 | 
| L | BCB304 | 
| M | ILE69 | 
| M | MET120 | 
| M | PHE148 | 
| M | PHE154 | 
| M | VAL155 | 
| M | LEU184 | 
| M | PHE187 | 
| M | SER188 | 
| M | PHE194 | 
| M | TYR195 | 
| M | HIS200 | 
| M | SER203 | 
| M | ILE204 | 
| M | TYR208 | 
| M | MET275 | 
| M | ALA278 | 
| M | ILE282 | 
| M | BPB404 | 
| site_id | AE6 | 
| Number of Residues | 16 | 
| Details | binding site for residue BPB M 404 | 
| Chain | Residue | 
| L | PHE181 | 
| L | MET185 | 
| L | LEU189 | 
| L | VAL220 | 
| L | BCB304 | 
| M | PHE59 | 
| M | SER123 | 
| M | LEU124 | 
| M | TRP127 | 
| M | VAL131 | 
| M | ILE144 | 
| M | ASN147 | 
| M | PHE148 | 
| M | SER271 | 
| M | MET275 | 
| M | BCB403 | 
| site_id | AE7 | 
| Number of Residues | 9 | 
| Details | binding site for residue NS5 M 405 | 
| Chain | Residue | 
| L | BCB304 | 
| M | LEU114 | 
| M | GLY117 | 
| M | LEU118 | 
| M | MET120 | 
| M | THR121 | 
| M | GLY159 | 
| M | GLY176 | 
| M | HIS180 | 
| site_id | AE8 | 
| Number of Residues | 7 | 
| Details | binding site for residue SO4 M 406 | 
| Chain | Residue | 
| M | TRP23 | 
| M | TYR50 | 
| M | GLY52 | 
| M | ALA53 | 
| M | SER54 | 
| M | SER133 | 
| M | HOH502 | 
| site_id | AE9 | 
| Number of Residues | 3 | 
| Details | binding site for residue SO4 M 407 | 
| Chain | Residue | 
| H | LEU246 | 
| M | ALA1 | 
| M | ARG226 | 
| site_id | AF1 | 
| Number of Residues | 3 | 
| Details | binding site for residue SO4 M 408 | 
| Chain | Residue | 
| L | ASN199 | 
| M | HIS143 | 
| M | ARG265 | 
| site_id | AF2 | 
| Number of Residues | 3 | 
| Details | binding site for residue SO4 M 409 | 
| Chain | Residue | 
| M | SER35 | 
| M | TYR36 | 
| M | TRP37 | 
| site_id | AF3 | 
| Number of Residues | 2 | 
| Details | binding site for residue SO4 M 410 | 
| Chain | Residue | 
| M | LEU107 | 
| M | HIS108 | 
| site_id | AF4 | 
| Number of Residues | 6 | 
| Details | binding site for residue SO4 M 411 | 
| Chain | Residue | 
| H | ASP202 | 
| H | VAL203 | 
| H | LYS204 | 
| M | TYR3 | 
| M | TYR7 | 
| M | GLN9 | 
| site_id | AF5 | 
| Number of Residues | 4 | 
| Details | binding site for residue SO4 M 412 | 
| Chain | Residue | 
| M | GLY14 | 
| M | HIS16 | 
| M | PRO32 | 
| M | TYR34 | 
Functional Information from PROSITE/UniProt
| site_id | PS00244 | 
| Number of Residues | 27 | 
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NwhynPgHmsSvsflfvnamalGlHGG | 
| Chain | Residue | Details | 
| L | ASN166-GLY192 | |
| M | ASN193-ALA219 | 
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 | 260 | 
| Details | Transmembrane: {"description":"Helical"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 147 | 
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]} | 
| 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 | 











