3D38
Crystal structure of new trigonal form of photosynthetic reaction center from Blastochloris viridis. Crystals grown in microfluidics by detergent capture.
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 | 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 |
H | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
L | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
L | 0015979 | biological_process | photosynthesis |
L | 0016020 | cellular_component | membrane |
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 | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
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 | 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 | 0045156 | molecular_function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity |
M | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 M 500 |
Chain | Residue |
L | HIS190 |
L | HIS230 |
M | HIS217 |
M | GLU232 |
M | HIS264 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 M 801 |
Chain | Residue |
L | ASN199 |
M | HIS143 |
M | ARG265 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 M 802 |
Chain | Residue |
M | TYR50 |
M | GLY52 |
M | ALA53 |
M | SER54 |
M | SER133 |
M | TRP23 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 H 803 |
Chain | Residue |
H | THR250 |
H | ARG253 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 M 804 |
Chain | Residue |
H | LEU246 |
M | ALA1 |
M | ARG226 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 M 805 |
Chain | Residue |
M | SER35 |
M | TYR36 |
M | TRP37 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 806 |
Chain | Residue |
H | ARG37 |
H | TYR41 |
H | GLU61 |
M | ARG251 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 807 |
Chain | Residue |
H | TYR117 |
H | GLU119 |
H | ARG233 |
H | LYS237 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 808 |
Chain | Residue |
C | ALA319 |
C | SER320 |
C | ARG321 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 809 |
Chain | Residue |
C | GLU112 |
C | ARG115 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 810 |
Chain | Residue |
C | ASN196 |
C | LYS198 |
C | ARG199 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 811 |
Chain | Residue |
C | HIS162 |
C | ARG165 |
L | ASP70 |
L | LYS72 |
L | TYR73 |
L | GLU82 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 H 812 |
Chain | Residue |
H | HIS72 |
H | ASP129 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 813 |
Chain | Residue |
C | THR161 |
C | HIS162 |
L | LYS72 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 814 |
Chain | Residue |
C | LYS258 |
C | ARG293 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 815 |
Chain | Residue |
C | PRO160 |
C | ARG165 |
M | PRO306 |
site_id | BC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEC C 401 |
Chain | Residue |
C | TYR56 |
C | LYS57 |
C | ASN58 |
C | LYS60 |
C | LEU62 |
C | PHE70 |
C | LEU71 |
C | MET74 |
C | THR75 |
C | ILE77 |
C | THR78 |
C | CYS87 |
C | CYS90 |
C | HIS91 |
C | LEU96 |
C | ALA97 |
C | TYR104 |
C | ALA107 |
C | ARG108 |
site_id | BC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEC C 402 |
Chain | Residue |
C | TYR89 |
C | TYR102 |
C | MET110 |
C | LEU111 |
C | MET113 |
C | THR114 |
C | THR131 |
C | CYS132 |
C | CYS135 |
C | HIS136 |
C | PRO140 |
C | LEU141 |
C | PRO142 |
C | ARG293 |
C | PRO301 |
site_id | CC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEC C 403 |
Chain | Residue |
C | PHE253 |
C | GLU254 |
C | ARG264 |
C | ALA267 |
C | TRP268 |
C | ARG272 |
M | ILE189 |
C | ARG202 |
C | PHE230 |
C | MET233 |
C | MET234 |
C | ILE236 |
C | SER237 |
C | LEU240 |
C | ASN243 |
C | CYS244 |
C | CYS247 |
C | HIS248 |
site_id | CC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HEC C 404 |
Chain | Residue |
C | HIS124 |
C | THR128 |
C | ILE236 |
C | LEU240 |
C | PHE246 |
C | GLN263 |
C | ILE266 |
C | GLY270 |
C | ILE271 |
C | MET273 |
C | CYS305 |
C | CYS308 |
C | HIS309 |
C | THR313 |
C | LYS314 |
C | PRO315 |
site_id | CC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BCB L 400 |
Chain | Residue |
L | PHE97 |
L | PRO124 |
L | MET127 |
L | PHE128 |
L | ASN158 |
L | PHE160 |
L | GLY161 |
L | TYR162 |
L | TRP167 |
L | HIS168 |
L | HIS173 |
L | SER176 |
L | ILE240 |
L | PHE241 |
L | GLY244 |
L | THR248 |
M | TYR195 |
M | TYR208 |
site_id | CC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BCB L 401 |
Chain | Residue |
L | PHE128 |
L | PHE146 |
L | ILE150 |
L | HIS153 |
L | LEU154 |
M | GLY201 |
M | ILE204 |
M | GLY205 |
M | TYR208 |
M | GLY209 |
site_id | CC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BPB L 402 |
Chain | Residue |
L | PHE41 |
L | ILE42 |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | PHE121 |
L | PRO124 |
L | TYR148 |
L | GLY149 |
L | ILE150 |
L | HIS153 |
L | ALA237 |
L | PHE241 |
M | TYR208 |
M | GLY211 |
M | LEU212 |
M | TRP250 |
site_id | CC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MQ9 M 501 |
Chain | Residue |
L | TYR29 |
L | ILE39 |
L | PHE43 |
L | TRP100 |
M | HIS217 |
M | ALA246 |
M | TRP250 |
M | ILE254 |
M | ASN257 |
M | ALA258 |
M | TRP266 |
site_id | CC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE UQ1 L 502 |
Chain | Residue |
L | LEU189 |
L | HIS190 |
L | LEU193 |
L | GLU212 |
L | ASN213 |
L | PHE216 |
L | SER223 |
L | ILE224 |
L | GLY225 |
L | ILE229 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE UQ1 L 503 |
Chain | Residue |
L | TRP266 |
M | PHE85 |
M | PHE88 |
M | PHE89 |
site_id | CC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BCB M 400 |
Chain | Residue |
L | HIS168 |
L | MET174 |
L | SER178 |
L | PHE181 |
L | MET185 |
M | ILE177 |
M | TRP178 |
M | HIS180 |
M | ILE181 |
M | LEU184 |
site_id | DC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BCB M 401 |
Chain | Residue |
L | TYR162 |
L | PHE181 |
M | GLY62 |
M | LEU124 |
M | PHE154 |
M | LEU184 |
M | THR185 |
M | PHE187 |
M | SER188 |
M | PHE194 |
M | TYR195 |
M | HIS200 |
M | SER203 |
M | ILE204 |
M | TYR208 |
M | MET275 |
M | ALA278 |
M | ILE282 |
site_id | DC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BPB M 402 |
Chain | Residue |
L | PHE181 |
L | ALA184 |
L | MET185 |
L | LEU189 |
M | ALA58 |
M | PHE59 |
M | SER123 |
M | LEU124 |
M | TRP127 |
M | ILE144 |
M | ASN147 |
M | PHE148 |
M | SER271 |
site_id | DC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NS5 M 600 |
Chain | Residue |
M | LEU70 |
M | LEU114 |
M | GLY117 |
M | THR121 |
M | GLY159 |
M | CYS160 |
M | PHE175 |
M | GLY176 |
M | ILE177 |
M | HIS180 |
site_id | DC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE LDA H 701 |
Chain | Residue |
H | ARG33 |
H | ASP56 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LDA L 702 |
Chain | Residue |
H | TRP17 |
L | ASP60 |
M | TYR195 |
M | PRO198 |
M | TRP295 |
M | HIS299 |
site_id | DC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA H 703 |
Chain | Residue |
H | LEU30 |
H | ARG34 |
H | TYR60 |
H | LEU62 |
H | TYR64 |
site_id | DC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE LDA M 704 |
Chain | Residue |
M | ALA53 |
M | LEU122 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE HTO H 705 |
Chain | Residue |
H | PRO71 |
H | HIS72 |
H | ASP125 |
H | ALA126 |
site_id | DC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE HTO C 706 |
Chain | Residue |
C | PRO205 |
C | GLN206 |
C | ARG221 |
site_id | EC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE HTO C 707 |
Chain | Residue |
C | GLU21 |
C | GLY241 |
C | THR313 |
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 | 88 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:2676514 |
Chain | Residue | Details |
M | ALA1-TYR50 | |
M | ALA137-GLY141 | |
M | ALA223-ALA258 | |
C | HIS124 | |
C | HIS136 | |
C | MET233 | |
C | HIS248 | |
C | HIS309 |
site_id | SWS_FT_FI2 |
Number of Residues | 122 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
M | LEU51-ALA75 | |
M | GLY110-ARG136 | |
M | THR142-LEU165 | |
M | CYS197-LEU222 | |
M | THR259-LEU283 | |
C | CYS247 | |
C | CYS305 | |
C | CYS308 |
site_id | SWS_FT_FI3 |
Number of Residues | 102 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:2676514 |
Chain | Residue | Details |
M | GLU76-ASP109 | |
M | VAL166-TYR196 | |
M | LEU284-LYS323 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
M | HIS180 | |
M | HIS200 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
M | HIS217 | |
M | GLU232 | |
M | HIS264 | |
M | TRP250 |