1L9J
X-Ray Structure of the Cytochrome-c(2)-Photosynthetic Reaction Center Electron Transfer Complex from Rhodobacter sphaeroides in Type I Co-Crystals
Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0009055 | molecular_function | electron transfer activity |
C | 0015979 | biological_process | photosynthesis |
C | 0020037 | molecular_function | heme binding |
C | 0042597 | cellular_component | periplasmic space |
C | 0046872 | molecular_function | metal ion binding |
D | 0009055 | molecular_function | electron transfer activity |
D | 0015979 | biological_process | photosynthesis |
D | 0020037 | molecular_function | heme binding |
D | 0042597 | cellular_component | periplasmic space |
D | 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 |
R | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
R | 0015979 | biological_process | photosynthesis |
R | 0016020 | cellular_component | membrane |
R | 0016168 | molecular_function | chlorophyll binding |
R | 0019684 | biological_process | photosynthesis, light reaction |
R | 0030077 | cellular_component | plasma membrane light-harvesting complex |
R | 0042314 | molecular_function | bacteriochlorophyll binding |
R | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
R | 0046872 | molecular_function | metal ion binding |
S | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
S | 0015979 | biological_process | photosynthesis |
S | 0016020 | cellular_component | membrane |
S | 0016168 | molecular_function | chlorophyll binding |
S | 0019684 | biological_process | photosynthesis, light reaction |
S | 0030077 | cellular_component | plasma membrane light-harvesting complex |
S | 0042314 | molecular_function | bacteriochlorophyll binding |
S | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
S | 0046872 | molecular_function | metal ion binding |
T | 0015979 | biological_process | photosynthesis |
T | 0016020 | cellular_component | membrane |
T | 0016168 | molecular_function | chlorophyll binding |
T | 0019684 | biological_process | photosynthesis, light reaction |
T | 0030077 | cellular_component | plasma membrane light-harvesting complex |
T | 0042314 | molecular_function | bacteriochlorophyll binding |
T | 0042717 | cellular_component | plasma membrane-derived chromatophore membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 M 1007 |
Chain | Residue |
L | HIS190 |
L | HIS230 |
M | HIS219 |
M | GLU234 |
M | HIS266 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 S 2007 |
Chain | Residue |
S | HIS266 |
R | HIS190 |
R | HIS230 |
S | HIS219 |
S | GLU234 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL S 2012 |
Chain | Residue |
S | HIS145 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BCL M 1001 |
Chain | Residue |
L | HIS168 |
L | MET174 |
L | ILE177 |
L | SER178 |
L | PHE181 |
L | THR182 |
L | BCL1002 |
L | BPH1005 |
M | TRP157 |
M | HIS182 |
M | LEU183 |
M | THR186 |
M | BCL1003 |
M | LDA1011 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE BCL L 1002 |
Chain | Residue |
L | PHE97 |
L | ALA124 |
L | TYR128 |
L | LEU131 |
L | VAL157 |
L | TYR162 |
L | PHE167 |
L | HIS168 |
L | HIS173 |
L | ILE177 |
L | PHE180 |
L | SER244 |
L | ALA245 |
L | CYS247 |
L | MET248 |
L | BCL1004 |
M | TYR210 |
M | BCL1001 |
M | BCL1003 |
M | BPH1006 |
site_id | AC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE BCL M 1003 |
Chain | Residue |
L | TYR162 |
L | PHE181 |
L | BCL1002 |
L | BCL1004 |
L | BPH1005 |
M | TRP66 |
M | ALA153 |
M | LEU156 |
M | TRP157 |
M | THR186 |
M | ASN187 |
M | SER190 |
M | LEU196 |
M | PHE197 |
M | HIS202 |
M | SER205 |
M | ILE206 |
M | TYR210 |
M | GLY280 |
M | GLY281 |
M | ILE284 |
M | BCL1001 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BCL L 1004 |
Chain | Residue |
L | ILE46 |
L | ILE49 |
L | TYR128 |
L | LEU131 |
L | ILE150 |
L | TRP151 |
L | HIS153 |
L | LEU154 |
L | BCL1002 |
M | PHE197 |
M | GLY203 |
M | ILE206 |
M | ALA207 |
M | TYR210 |
M | LEU214 |
M | BCL1003 |
M | BPH1006 |
M | LDA1010 |
M | HOH1025 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BPH L 1005 |
Chain | Residue |
M | BCL1001 |
M | BCL1003 |
L | PHE181 |
L | ALA184 |
L | LEU185 |
L | LEU189 |
L | LEU219 |
M | GLY63 |
M | TRP129 |
M | THR146 |
M | ALA149 |
M | PHE150 |
M | ALA153 |
M | ALA273 |
M | THR277 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE BPH M 1006 |
Chain | Residue |
L | ILE46 |
L | ALA93 |
L | PHE97 |
L | TRP100 |
L | GLU104 |
L | ILE117 |
L | PHE121 |
L | TYR148 |
L | HIS153 |
L | LEU238 |
L | VAL241 |
L | BCL1002 |
L | BCL1004 |
M | TYR210 |
M | ALA213 |
M | LEU214 |
M | MET218 |
M | TRP252 |
M | MET256 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE U10 M 1008 |
Chain | Residue |
L | TRP100 |
M | MET218 |
M | HIS219 |
M | THR222 |
M | ILE223 |
M | ALA249 |
M | TRP252 |
M | MET256 |
M | ASN259 |
M | ALA260 |
M | THR261 |
M | MET262 |
M | ILE265 |
M | TRP268 |
site_id | BC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEM C 1009 |
Chain | Residue |
C | CYS15 |
C | CYS18 |
C | HIS19 |
C | PRO38 |
C | ARG46 |
C | ALA48 |
C | GLY49 |
C | PHE54 |
C | TYR57 |
C | GLY58 |
C | MET61 |
C | TRP71 |
C | PHE76 |
C | TYR79 |
C | VAL80 |
C | LYS99 |
C | MET100 |
C | THR101 |
C | PHE102 |
M | LEU191 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA M 1010 |
Chain | Residue |
L | BCL1004 |
M | LEU204 |
M | MET272 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LDA M 1011 |
Chain | Residue |
M | PHE67 |
M | PHE74 |
M | MET122 |
M | TRP157 |
M | VAL175 |
M | PRO176 |
M | GLY178 |
M | HIS182 |
M | BCL1001 |
site_id | BC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BCL S 2001 |
Chain | Residue |
R | HIS168 |
R | MET174 |
R | ILE177 |
R | SER178 |
R | THR182 |
S | ILE179 |
S | HIS182 |
S | LEU183 |
S | THR186 |
S | BCL2003 |
S | LDA2011 |
site_id | BC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BCL R 2002 |
Chain | Residue |
R | PHE97 |
R | ALA124 |
R | TYR128 |
R | LEU131 |
R | VAL157 |
R | TYR162 |
R | PHE167 |
R | HIS168 |
R | HIS173 |
R | ILE177 |
R | PHE180 |
R | SER244 |
R | ALA245 |
R | CYS247 |
R | MET248 |
R | BCL2004 |
S | BCL2003 |
S | BPH2006 |
site_id | BC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE BCL S 2003 |
Chain | Residue |
R | VAL157 |
R | TYR162 |
R | PHE181 |
R | BCL2002 |
R | BPH2005 |
S | TRP66 |
S | ALA153 |
S | LEU156 |
S | TRP157 |
S | ASN187 |
S | PHE189 |
S | SER190 |
S | LEU196 |
S | PHE197 |
S | HIS202 |
S | SER205 |
S | ILE206 |
S | LEU209 |
S | TYR210 |
S | GLY280 |
S | ILE284 |
S | BCL2001 |
site_id | BC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BCL R 2004 |
Chain | Residue |
R | ILE46 |
R | ILE49 |
R | TYR128 |
R | LEU131 |
R | PHE146 |
R | ILE150 |
R | TRP151 |
R | HIS153 |
R | LEU154 |
R | BCL2002 |
S | PHE197 |
S | GLY203 |
S | ILE206 |
S | ALA207 |
S | TYR210 |
S | LEU214 |
S | BPH2006 |
S | LDA2010 |
site_id | BC9 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BPH R 2005 |
Chain | Residue |
R | PHE181 |
R | ALA184 |
R | LEU185 |
R | LEU189 |
R | LEU219 |
S | SER59 |
S | LEU60 |
S | GLY63 |
S | LEU64 |
S | ALA125 |
S | TRP129 |
S | ALA149 |
S | PHE150 |
S | ALA153 |
S | ALA273 |
S | BCL2003 |
site_id | CC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE BPH S 2006 |
Chain | Residue |
R | ALA42 |
R | ILE49 |
R | ALA93 |
R | ALA96 |
R | PHE97 |
R | TRP100 |
R | GLU104 |
R | ILE117 |
R | ALA120 |
R | PHE121 |
R | TYR128 |
R | TYR148 |
R | LEU238 |
R | VAL241 |
R | BCL2002 |
R | BCL2004 |
S | TYR210 |
S | ALA213 |
S | LEU214 |
S | MET218 |
S | TRP252 |
S | MET256 |
site_id | CC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE U10 S 2008 |
Chain | Residue |
R | TRP100 |
S | HIS219 |
S | THR222 |
S | ALA249 |
S | TRP252 |
S | PHE258 |
S | ASN259 |
S | ALA260 |
S | THR261 |
S | MET262 |
S | TRP268 |
site_id | CC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM D 2009 |
Chain | Residue |
D | CYS15 |
D | CYS18 |
D | HIS19 |
D | THR36 |
D | PRO38 |
D | ARG46 |
D | ALA48 |
D | GLY49 |
D | PHE54 |
D | TYR57 |
D | GLY58 |
D | MET61 |
D | TRP71 |
D | PHE76 |
D | TYR79 |
D | LYS99 |
D | MET100 |
D | THR101 |
D | PHE102 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA S 2010 |
Chain | Residue |
R | BCL2004 |
S | PRO200 |
S | LEU204 |
S | PHE208 |
T | ILE28 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE LDA S 2011 |
Chain | Residue |
S | PHE74 |
S | MET122 |
S | VAL175 |
S | PRO176 |
S | GLY178 |
S | HIS182 |
S | BCL2001 |
Functional Information from PROSITE/UniProt
site_id | PS00244 |
Number of Residues | 27 |
Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NlfynPfHglSiaflygsallfAmHGA |
Chain | Residue | Details |
M | ASN195-ALA221 | |
L | ASN166-ALA192 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 116 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 556 |
Details | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 174 |
Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | Binding site: {"description":"axial binding residue"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 14 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"description":"covalent"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"8827449","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |