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: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU37 | |
B | TYR50 | |
B | VAL90 | |
B | PHE124 | |
B | ASP285 | |
B | THR326 | |
A | GLN45 | |
A | TYR50 | |
A | VAL90 | |
A | PHE124 | |
A | ASP285 | |
A | THR326 | |
B | GLU37 | |
B | GLN45 |