1PRC
CRYSTALLOGRAPHIC REFINEMENT AT 2.3 ANGSTROMS RESOLUTION AND REFINED MODEL OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS
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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 607 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS217 |
| M | GLU232 |
| M | HIS264 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 H 617 |
| Chain | Residue |
| M | ARG251 |
| H | ARG33 |
| H | ARG37 |
| H | TYR41 |
| H | HOH659 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 M 618 |
| Chain | Residue |
| L | ASN199 |
| M | HIS143 |
| M | ARG265 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 M 619 |
| Chain | Residue |
| H | LEU246 |
| M | ALA1 |
| M | ARG226 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 M 620 |
| Chain | Residue |
| M | TRP23 |
| M | TYR50 |
| M | ALA53 |
| M | SER54 |
| M | SER133 |
| M | HOH666 |
| M | HOH676 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 M 621 |
| Chain | Residue |
| M | SER35 |
| M | TYR36 |
| M | TRP37 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 H 622 |
| Chain | Residue |
| H | TYR117 |
| H | ARG233 |
| H | LYS237 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 H 623 |
| Chain | Residue |
| H | ARG34 |
| H | ARG34 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCB M 601 |
| Chain | Residue |
| L | HIS168 |
| L | MET174 |
| L | SER178 |
| L | PHE181 |
| L | VAL182 |
| L | MET185 |
| L | HOH635 |
| M | MET120 |
| M | VAL155 |
| M | TRP178 |
| M | HIS180 |
| M | ILE181 |
| M | BCB603 |
| M | BPB605 |
| M | NS1613 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BCB L 602 |
| Chain | Residue |
| L | PHE97 |
| L | PRO124 |
| L | MET127 |
| L | VAL157 |
| L | PHE160 |
| L | TRP167 |
| L | HIS168 |
| L | HIS173 |
| L | SER176 |
| L | VAL177 |
| L | PHE241 |
| L | GLY244 |
| L | THR248 |
| L | BCB604 |
| L | BPB606 |
| M | TYR195 |
| M | TYR208 |
| M | BCB603 |
| M | MQ7608 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BCB M 603 |
| Chain | Residue |
| L | TYR162 |
| L | PHE181 |
| L | BCB602 |
| L | BCB604 |
| M | MET120 |
| M | PHE148 |
| M | PHE154 |
| M | VAL155 |
| M | LEU184 |
| M | SER188 |
| M | PHE194 |
| M | TYR195 |
| M | HIS200 |
| M | SER203 |
| M | ILE204 |
| M | TYR208 |
| M | MET275 |
| M | ALA278 |
| M | BCB601 |
| M | BPB605 |
| site_id | BC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BCB L 604 |
| Chain | Residue |
| L | PHE146 |
| L | ILE150 |
| L | HIS153 |
| L | BCB602 |
| L | BPB606 |
| M | GLY201 |
| M | ILE204 |
| M | GLY205 |
| M | TYR208 |
| M | GLY209 |
| M | BCB603 |
| M | MQ7608 |
| M | HOH645 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BPB M 605 |
| Chain | Residue |
| L | MET185 |
| L | LEU189 |
| L | VAL220 |
| M | ILE66 |
| M | SER123 |
| M | LEU124 |
| M | TRP127 |
| M | ILE144 |
| M | PHE148 |
| M | SER271 |
| M | MET275 |
| M | BCB601 |
| M | BCB603 |
| L | PHE181 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BPB L 606 |
| Chain | Residue |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | PHE121 |
| L | PRO124 |
| L | TYR148 |
| L | HIS153 |
| L | ALA237 |
| L | PHE241 |
| L | BCB602 |
| L | BCB604 |
| M | TYR208 |
| M | LEU212 |
| M | TRP250 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MQ7 M 608 |
| Chain | Residue |
| L | TYR29 |
| L | BCB602 |
| L | BCB604 |
| M | ALA216 |
| M | HIS217 |
| M | THR220 |
| M | TRP250 |
| M | ALA258 |
| M | THR259 |
| site_id | BC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC C 609 |
| Chain | Residue |
| C | TYR56 |
| C | LYS57 |
| C | ASN58 |
| C | VAL59 |
| C | LYS60 |
| C | VAL61 |
| C | LEU62 |
| C | PHE70 |
| C | MET74 |
| C | ILE77 |
| C | THR78 |
| C | SER82 |
| C | CYS87 |
| C | CYS90 |
| C | HIS91 |
| C | LEU96 |
| C | ALA97 |
| C | TYR104 |
| C | ALA107 |
| C | ARG108 |
| C | VAL212 |
| site_id | BC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEC C 610 |
| Chain | Residue |
| C | TYR89 |
| C | TYR102 |
| C | VAL106 |
| C | MET110 |
| C | LEU111 |
| C | MET113 |
| C | THR114 |
| C | CYS132 |
| C | CYS135 |
| C | HIS136 |
| C | PRO140 |
| C | LEU141 |
| C | PRO142 |
| C | LEU289 |
| C | ARG293 |
| C | PRO301 |
| site_id | BC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC C 611 |
| Chain | Residue |
| C | VAL201 |
| C | ARG202 |
| C | VAL203 |
| C | VAL204 |
| C | MET233 |
| C | SER237 |
| C | THR242 |
| C | ASN243 |
| C | CYS244 |
| C | CYS247 |
| C | HIS248 |
| C | PHE253 |
| C | GLU254 |
| C | ARG264 |
| C | ALA267 |
| C | TRP268 |
| C | ARG272 |
| C | HOH638 |
| C | HOH639 |
| C | HOH640 |
| C | HOH666 |
| M | ILE189 |
| site_id | CC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC C 612 |
| Chain | Residue |
| C | HIS124 |
| C | THR128 |
| C | ILE236 |
| C | LEU240 |
| C | GLN263 |
| C | ILE266 |
| C | ALA267 |
| C | GLY270 |
| C | MET273 |
| C | VAL274 |
| C | ASP304 |
| C | CYS305 |
| C | CYS308 |
| C | HIS309 |
| C | LYS314 |
| C | PRO315 |
| C | HOH657 |
| C | HOH676 |
| site_id | CC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NS1 M 613 |
| Chain | Residue |
| M | GLY117 |
| M | THR121 |
| M | VAL155 |
| M | GLY159 |
| M | CYS160 |
| M | VAL173 |
| M | PRO174 |
| M | GLY176 |
| M | ILE177 |
| M | HIS180 |
| M | BCB601 |
| site_id | CC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE UQ1 L 614 |
| Chain | Residue |
| L | LEU189 |
| L | HIS190 |
| L | LEU193 |
| L | GLU212 |
| L | ASN213 |
| L | PHE216 |
| L | TYR222 |
| L | SER223 |
| L | ILE224 |
| L | GLY225 |
| L | ALA226 |
| L | ILE229 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LDA M 615 |
| Chain | Residue |
| H | ARG33 |
| H | PRO54 |
| H | ASP56 |
| M | GLY205 |
| M | PHE256 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA H 616 |
| Chain | Residue |
| L | LEU151 |
| M | TYR195 |
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 | 10 |
| Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:2676514 |
| Chain | Residue | Details |
| H | FME1-ASP11 | |
| M | LEU138-THR142 | |
| M | VAL224-THR259 | |
| C | HIS124 | |
| C | HIS136 | |
| C | MET233 | |
| C | HIS248 | |
| C | HIS309 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| H | ILE12-LEU30 | |
| M | GLY111-ALA137 | |
| M | HIS143-VAL166 | |
| M | PRO198-ALA223 | |
| M | ILE260-LEU284 | |
| C | CYS247 | |
| C | CYS305 | |
| C | CYS308 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 227 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:2676514 |
| Chain | Residue | Details |
| H | TYR31-LEU258 | |
| M | GLY167-CYS197 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:16453623 |
| Chain | Residue | Details |
| H | FME1 | |
| M | GLY201 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| M | GLY218 | |
| M | ILE233 | |
| M | ARG251 | |
| M | ARG265 |
