1FNP
CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT REACTION CENTER PRO L209-> PHE FROM THE PHOTOSYNTHETIC PURPLE BACTERIUM RHODOBACTER SPHAEROIDES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 500 |
| Chain | Residue |
| L | HIS190 |
| L | HIS230 |
| M | HIS218 |
| M | GLU233 |
| M | HIS265 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 M 800 |
| Chain | Residue |
| L | ASN199 |
| M | HIS144 |
| M | ARG266 |
| M | LDA704 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BCL M 801 |
| Chain | Residue |
| L | HIS168 |
| L | MET174 |
| L | ILE177 |
| L | SER178 |
| L | THR182 |
| L | BCL302 |
| M | PHE89 |
| M | ILE178 |
| M | HIS181 |
| M | LEU182 |
| M | THR185 |
| M | BPH401 |
| M | SPO600 |
| M | BCL802 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BCL L 302 |
| Chain | Residue |
| L | PHE97 |
| L | ALA124 |
| L | ILE125 |
| L | ALA127 |
| L | TYR128 |
| L | LEU131 |
| L | TRP156 |
| L | ASN166 |
| L | PHE167 |
| L | HIS168 |
| L | HIS173 |
| L | ILE177 |
| L | SER244 |
| L | CYS247 |
| L | MET248 |
| L | BCL304 |
| L | BPH402 |
| M | TYR209 |
| M | BCL801 |
| M | BCL802 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE BCL M 802 |
| Chain | Residue |
| L | VAL157 |
| L | BCL302 |
| L | BCL304 |
| M | MET121 |
| M | VAL125 |
| M | ALA152 |
| M | LEU155 |
| M | LEU159 |
| M | THR185 |
| M | ASN186 |
| M | PHE188 |
| M | SER189 |
| M | LEU195 |
| M | PHE196 |
| M | HIS201 |
| M | SER204 |
| M | ILE205 |
| M | TYR209 |
| M | VAL275 |
| M | GLY279 |
| M | ILE283 |
| M | BPH401 |
| M | BCL801 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCL L 304 |
| Chain | Residue |
| L | TYR128 |
| L | HIS153 |
| L | LEU154 |
| L | BCL302 |
| M | GLY202 |
| M | ILE205 |
| M | ALA206 |
| M | TYR209 |
| M | U10501 |
| M | LDA701 |
| M | BCL802 |
| M | HOH806 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BPH M 401 |
| Chain | Residue |
| L | PHE181 |
| L | ALA184 |
| L | LEU185 |
| L | LEU189 |
| M | SER58 |
| M | GLY62 |
| M | ALA124 |
| M | TRP128 |
| M | THR145 |
| M | PHE149 |
| M | ALA152 |
| M | ALA272 |
| M | THR276 |
| M | BCL801 |
| M | BCL802 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BPH L 402 |
| Chain | Residue |
| L | ALA120 |
| L | PHE121 |
| L | ALA124 |
| L | TYR148 |
| L | LEU238 |
| L | VAL241 |
| L | BCL302 |
| M | TYR209 |
| M | ALA212 |
| M | LEU213 |
| M | MET217 |
| M | TRP251 |
| M | MET255 |
| L | PHE41 |
| L | ALA96 |
| L | PHE97 |
| L | TRP100 |
| L | GLU104 |
| L | ILE117 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE U10 M 501 |
| Chain | Residue |
| H | LDA702 |
| L | THR38 |
| L | TRP100 |
| L | BCL304 |
| M | MET217 |
| M | HIS218 |
| M | THR221 |
| M | ILE222 |
| M | ALA247 |
| M | ALA248 |
| M | TRP251 |
| M | MET255 |
| M | ASN258 |
| M | ALA259 |
| M | ILE264 |
| M | TRP267 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE U10 L 502 |
| Chain | Residue |
| L | PHE179 |
| L | ALA186 |
| L | LEU189 |
| L | HIS190 |
| L | LEU193 |
| L | PHE216 |
| L | SER223 |
| L | ILE224 |
| L | GLY225 |
| L | ILE229 |
| L | LEU232 |
| L | SER239 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SPO M 600 |
| Chain | Residue |
| M | PHE66 |
| M | ILE69 |
| M | GLY70 |
| M | TRP74 |
| M | TRP114 |
| M | SER118 |
| M | TRP156 |
| M | PHE161 |
| M | TYR176 |
| M | GLY177 |
| M | ILE178 |
| M | HIS181 |
| M | BCL801 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA M 701 |
| Chain | Residue |
| H | HOH756 |
| L | BCL304 |
| M | PRO199 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LDA H 702 |
| Chain | Residue |
| H | GLN32 |
| H | TYR40 |
| H | LEU42 |
| M | ARG252 |
| M | GLY256 |
| M | U10501 |
| M | LDA703 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA M 703 |
| Chain | Residue |
| H | LDA702 |
| L | PRO28 |
| M | GLY256 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LDA M 704 |
| Chain | Residue |
| H | LDA706 |
| M | HIS144 |
| M | ARG266 |
| M | TRP270 |
| M | PO4800 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LDA L 705 |
| Chain | Residue |
| L | ILE150 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA H 706 |
| Chain | Residue |
| H | PHE23 |
| H | LEU27 |
| H | TYR30 |
| M | LDA704 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA M 707 |
| Chain | Residue |
| L | VAL220 |
| L | GLY221 |
| M | GLY30 |
| M | LEU46 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NfhynPaHmiAisffftnalalAlHGA |
| Chain | Residue | Details |
| L | ASN166-ALA192 | |
| M | ASN194-ALA220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 278 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 87 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Binding site: {} |
| Chain | Residue | Details |






