3LZX
Crystal structure of ferredoxin-NADP+ oxidoreductase from Bacillus subtilis (FORM II)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD A 1000 |
| Chain | Residue |
| A | ILE13 |
| A | GLN45 |
| A | LEU46 |
| A | TYR50 |
| A | ASP57 |
| A | GLN88 |
| A | ALA89 |
| A | VAL90 |
| A | THR118 |
| A | ALA119 |
| A | GLY120 |
| A | GLY14 |
| A | GLY122 |
| A | ALA123 |
| A | PHE124 |
| A | GLY284 |
| A | ASP285 |
| A | LEU295 |
| A | ILE296 |
| A | HOH333 |
| A | HOH343 |
| A | HOH347 |
| A | GLY16 |
| A | HOH375 |
| A | HOH413 |
| B | HIS324 |
| B | SER325 |
| B | THR326 |
| A | PRO17 |
| A | VAL18 |
| A | ILE36 |
| A | GLU37 |
| A | SER38 |
| A | GLY44 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAP A 2000 |
| Chain | Residue |
| A | GLY162 |
| A | GLY163 |
| A | ASP164 |
| A | SER165 |
| A | ASP168 |
| A | HIS184 |
| A | ARG185 |
| A | ARG186 |
| A | ARG190 |
| A | HIS192 |
| A | ASN245 |
| A | TYR246 |
| A | GLY247 |
| A | PHE248 |
| A | HOH359 |
| A | HOH382 |
| A | HOH387 |
| A | HOH449 |
| A | HOH451 |
| A | HOH483 |
| A | HOH491 |
| A | HOH521 |
| A | HOH526 |
| A | HOH551 |
| A | HOH556 |
| A | HOH563 |
| A | HOH592 |
| A | HOH596 |
| A | HOH601 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 3001 |
| Chain | Residue |
| A | SER266 |
| A | ASP285 |
| A | HOH346 |
| A | HOH440 |
| A | HOH614 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD B 1001 |
| Chain | Residue |
| B | HOH342 |
| B | HOH354 |
| B | HOH424 |
| A | HIS324 |
| A | SER325 |
| A | THR326 |
| B | ILE13 |
| B | GLY14 |
| B | GLY16 |
| B | PRO17 |
| B | VAL18 |
| B | ILE36 |
| B | GLU37 |
| B | SER38 |
| B | GLY44 |
| B | GLN45 |
| B | LEU46 |
| B | TYR50 |
| B | ASP57 |
| B | GLN88 |
| B | ALA89 |
| B | VAL90 |
| B | THR118 |
| B | ALA119 |
| B | GLY120 |
| B | GLY122 |
| B | ALA123 |
| B | PHE124 |
| B | GLY284 |
| B | ASP285 |
| B | LEU295 |
| B | ILE296 |
| B | HOH337 |
| B | HOH340 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP B 2001 |
| Chain | Residue |
| B | ALA48 |
| B | LEU49 |
| B | GLU52 |
| B | GLY162 |
| B | GLY163 |
| B | ASP164 |
| B | SER165 |
| B | ASP168 |
| B | HIS184 |
| B | ARG185 |
| B | ARG186 |
| B | ARG190 |
| B | HIS192 |
| B | ASN245 |
| B | TYR246 |
| B | GLY247 |
| B | HOH336 |
| B | HOH352 |
| B | HOH373 |
| B | HOH374 |
| B | HOH395 |
| B | HOH408 |
| B | HOH425 |
| B | HOH436 |
| B | HOH437 |
| B | HOH448 |
| B | HOH463 |
| B | HOH541 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 3002 |
| Chain | Residue |
| B | SER266 |
| B | ASP285 |
| B | HOH349 |
| B | HOH353 |
| B | HOH550 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
