2BGJ
X-Ray Structure of the Ferredoxin-NADP(H) Reductase from Rhodobacter capsulatus at 2.1 Angstroms
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042167 | biological_process | heme catabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042167 | biological_process | heme catabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0042167 | biological_process | heme catabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0042167 | biological_process | heme catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A1273 |
| Chain | Residue |
| A | PHE49 |
| A | GLY87 |
| A | PRO88 |
| A | LEU89 |
| A | THR90 |
| A | THR130 |
| A | ALA133 |
| A | LYS265 |
| A | ALA266 |
| A | PHE267 |
| A | GLY271 |
| A | ARG64 |
| A | ILE272 |
| A | HOH2021 |
| A | HOH2028 |
| A | HOH2040 |
| A | HOH2085 |
| A | HOH2086 |
| A | HOH2090 |
| A | HOH2091 |
| A | ALA65 |
| A | TYR66 |
| A | SER67 |
| A | TYR80 |
| A | SER81 |
| A | ILE82 |
| A | VAL84 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD B1273 |
| Chain | Residue |
| B | PHE49 |
| B | ARG64 |
| B | ALA65 |
| B | TYR66 |
| B | SER67 |
| B | TYR80 |
| B | SER81 |
| B | ILE82 |
| B | GLY87 |
| B | PRO88 |
| B | LEU89 |
| B | THR90 |
| B | THR130 |
| B | ALA133 |
| B | LYS265 |
| B | ALA266 |
| B | PHE267 |
| B | VAL268 |
| B | GLU270 |
| B | GLY271 |
| B | ILE272 |
| B | HOH2082 |
| B | HOH2083 |
| B | HOH2085 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD C1273 |
| Chain | Residue |
| C | ARG64 |
| C | ALA65 |
| C | TYR66 |
| C | SER67 |
| C | TYR80 |
| C | SER81 |
| C | ILE82 |
| C | VAL84 |
| C | GLY87 |
| C | PRO88 |
| C | LEU89 |
| C | THR90 |
| C | THR130 |
| C | ALA133 |
| C | LYS265 |
| C | ALA266 |
| C | PHE267 |
| C | VAL268 |
| C | GLU270 |
| C | GLY271 |
| C | ILE272 |
| C | HOH2076 |
| C | HOH2077 |
| C | HOH2079 |
| C | HOH2080 |
| C | HOH2081 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD D1273 |
| Chain | Residue |
| D | HOH2092 |
| D | HOH2093 |
| D | HOH2094 |
| D | ARG64 |
| D | ALA65 |
| D | TYR66 |
| D | SER67 |
| D | TYR80 |
| D | SER81 |
| D | ILE82 |
| D | GLY87 |
| D | PRO88 |
| D | LEU89 |
| D | THR90 |
| D | THR130 |
| D | ALA133 |
| D | LYS265 |
| D | ALA266 |
| D | PHE267 |
| D | VAL268 |
| D | GLU270 |
| D | GLY271 |
| D | ILE272 |
| D | HOH2018 |
| D | HOH2091 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470 |
| Chain | Residue | Details |
| D | ARG64 | |
| D | TYR80 | |
| D | PRO88 | |
| D | THR130 | |
| A | ARG64 | |
| A | TYR80 | |
| A | PRO88 | |
| A | THR130 | |
| B | ARG64 | |
| B | TYR80 | |
| B | PRO88 | |
| B | THR130 | |
| C | ARG64 | |
| C | TYR80 | |
| C | PRO88 | |
| C | THR130 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18973834 |
| Chain | Residue | Details |
| A | ASP240 | |
| B | THR128 | |
| B | ARG158 | |
| B | THR194 | |
| B | ARG203 | |
| B | ASP240 | |
| C | THR128 | |
| C | ARG158 | |
| C | THR194 | |
| C | ARG203 | |
| C | ASP240 | |
| D | THR128 | |
| D | ARG158 | |
| D | THR194 | |
| D | ARG203 | |
| D | ASP240 | |
| A | THR128 | |
| A | ARG158 | |
| A | THR194 | |
| A | ARG203 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:18973834 |
| Chain | Residue | Details |
| A | ALA266 | |
| B | ALA266 | |
| C | ALA266 | |
| D | ALA266 |
