6GAS
Crystal structure of oxidised ferredoxin/flavodoxin NADP+ oxidoreductase 2 (FNR2) from Bacillus cereus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0045454 | biological_process | cell redox homeostasis |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0045454 | biological_process | cell redox homeostasis |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | binding site for residue FAD A 1001 |
| Chain | Residue |
| A | ILE15 |
| A | LEU48 |
| A | TYR52 |
| A | ASP59 |
| A | GLU90 |
| A | ALA91 |
| A | VAL92 |
| A | THR120 |
| A | ALA121 |
| A | GLY122 |
| A | GLY124 |
| A | GLY16 |
| A | ALA125 |
| A | PHE126 |
| A | GLY286 |
| A | ASP287 |
| A | LEU297 |
| A | ILE298 |
| A | NA1002 |
| A | HOH1112 |
| A | HOH1127 |
| A | HOH1129 |
| A | GLY18 |
| B | HIS326 |
| B | SER327 |
| B | SER328 |
| C | ASN319 |
| A | PRO19 |
| A | THR20 |
| A | GLU39 |
| A | SER40 |
| A | GLY46 |
| A | GLN47 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 1002 |
| Chain | Residue |
| A | GLY16 |
| A | GLY18 |
| A | GLY21 |
| A | THR120 |
| A | FAD1001 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 1001 |
| Chain | Residue |
| A | HIS326 |
| A | SER327 |
| B | ILE15 |
| B | GLY16 |
| B | GLY18 |
| B | PRO19 |
| B | THR20 |
| B | ILE38 |
| B | GLU39 |
| B | SER40 |
| B | GLY46 |
| B | GLN47 |
| B | LEU48 |
| B | TYR52 |
| B | ASP59 |
| B | GLU90 |
| B | ALA91 |
| B | VAL92 |
| B | THR120 |
| B | ALA121 |
| B | GLY122 |
| B | GLY124 |
| B | ALA125 |
| B | PHE126 |
| B | GLY286 |
| B | ASP287 |
| B | LEU297 |
| B | ILE298 |
| B | HOH1108 |
| B | HOH1120 |
| B | HOH1128 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue NA B 1002 |
| Chain | Residue |
| B | MET202 |
| B | SER204 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | binding site for residue FAD C 1001 |
| Chain | Residue |
| C | HOH1111 |
| C | HOH1117 |
| C | HOH1130 |
| D | SER327 |
| D | SER328 |
| A | ASN319 |
| C | ILE15 |
| C | GLY16 |
| C | GLY18 |
| C | PRO19 |
| C | THR20 |
| C | GLU39 |
| C | SER40 |
| C | GLY46 |
| C | GLN47 |
| C | LEU48 |
| C | LEU51 |
| C | TYR52 |
| C | ILE57 |
| C | ASP59 |
| C | GLU90 |
| C | ALA91 |
| C | VAL92 |
| C | THR120 |
| C | ALA121 |
| C | GLY122 |
| C | GLY124 |
| C | ALA125 |
| C | PHE126 |
| C | ASP287 |
| C | LEU297 |
| C | ILE298 |
| C | NA1002 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue NA C 1002 |
| Chain | Residue |
| C | THR120 |
| C | ALA121 |
| C | GLY122 |
| C | ALA285 |
| C | GLY286 |
| C | ASP287 |
| C | ILE288 |
| C | FAD1001 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | binding site for residue FAD D 1001 |
| Chain | Residue |
| C | SER327 |
| D | ILE15 |
| D | GLY16 |
| D | GLY18 |
| D | PRO19 |
| D | THR20 |
| D | GLU39 |
| D | SER40 |
| D | GLY46 |
| D | GLN47 |
| D | LEU48 |
| D | TYR52 |
| D | ASP59 |
| D | GLU90 |
| D | ALA91 |
| D | VAL92 |
| D | THR120 |
| D | ALA121 |
| D | GLY122 |
| D | GLY124 |
| D | ALA125 |
| D | PHE126 |
| D | GLY286 |
| D | ASP287 |
| D | LEU297 |
| D | ILE298 |
| D | NA1002 |
| D | HOH1117 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 1002 |
| Chain | Residue |
| D | GLY16 |
| D | GLY18 |
| D | GLY21 |
| D | THR120 |
| D | FAD1001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01685 |
| Chain | Residue | Details |
| A | THR20 | |
| B | GLU39 | |
| B | GLN47 | |
| B | TYR52 | |
| B | VAL92 | |
| B | PHE126 | |
| B | ASP287 | |
| B | SER328 | |
| C | THR20 | |
| C | GLU39 | |
| C | GLN47 | |
| A | GLU39 | |
| C | TYR52 | |
| C | VAL92 | |
| C | PHE126 | |
| C | ASP287 | |
| C | SER328 | |
| D | THR20 | |
| D | GLU39 | |
| D | GLN47 | |
| D | TYR52 | |
| D | VAL92 | |
| A | GLN47 | |
| D | PHE126 | |
| D | ASP287 | |
| D | SER328 | |
| A | TYR52 | |
| A | VAL92 | |
| A | PHE126 | |
| A | ASP287 | |
| A | SER328 | |
| B | THR20 |
