7P2C
F(M197)H mutant structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV by fixed-target serial synchrotron crystallography (room temperature, 26keV)
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 PROSITE/UniProt
site_id | PS00244 |
Number of Residues | 27 |
Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NlhynPfHglSiaflygsallfAmHGA |
Chain | Residue | Details |
M | ASN195-ALA221 | |
L | ASN166-ALA192 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 278 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 58 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 87 |
Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |