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 |






