5J60
Structure of a thioredoxin reductase from Gloeobacter violaceus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0045454 | biological_process | cell redox homeostasis |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0045454 | biological_process | cell redox homeostasis |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | GLY12 |
| A | ALA42 |
| A | LEU43 |
| A | THR46 |
| A | ILE49 |
| A | ASN51 |
| A | ALA82 |
| A | VAL84 |
| A | THR112 |
| A | GLY113 |
| A | GLY277 |
| A | GLY14 |
| A | ASP278 |
| A | LYS285 |
| A | GLN286 |
| A | ALA287 |
| A | ALA290 |
| A | HOH520 |
| A | HOH536 |
| A | HOH550 |
| A | HOH553 |
| A | HOH564 |
| A | PRO15 |
| A | HOH572 |
| A | HOH586 |
| A | HOH599 |
| A | HOH617 |
| A | HOH631 |
| D | ASP314 |
| D | TRP315 |
| D | ALA316 |
| A | ALA16 |
| A | LEU34 |
| A | ASP35 |
| A | LYS36 |
| A | ASN37 |
| A | GLY41 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | GLU264 |
| A | PG4403 |
| D | GLU264 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue PG4 A 403 |
| Chain | Residue |
| A | VAL262 |
| A | ASP263 |
| A | GLU264 |
| A | CA402 |
| D | VAL262 |
| D | ASP263 |
| D | GLU264 |
| site_id | AC4 |
| Number of Residues | 39 |
| Details | binding site for residue FAD B 500 |
| Chain | Residue |
| B | GLY12 |
| B | GLY13 |
| B | GLY14 |
| B | PRO15 |
| B | ALA16 |
| B | LEU34 |
| B | ASP35 |
| B | LYS36 |
| B | ASN37 |
| B | GLY41 |
| B | ALA42 |
| B | LEU43 |
| B | THR46 |
| B | ILE49 |
| B | ASN51 |
| B | ALA82 |
| B | VAL84 |
| B | ALA111 |
| B | THR112 |
| B | GLY113 |
| B | GLY277 |
| B | ASP278 |
| B | LYS285 |
| B | GLN286 |
| B | ALA287 |
| B | ALA290 |
| B | HOH628 |
| B | HOH638 |
| B | HOH640 |
| B | HOH659 |
| B | HOH660 |
| B | HOH674 |
| B | HOH682 |
| B | HOH714 |
| B | HOH715 |
| C | TYR23 |
| C | ASP314 |
| C | TRP315 |
| C | ALA316 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue PG4 B 501 |
| Chain | Residue |
| B | VAL262 |
| B | ASP263 |
| B | GLU264 |
| B | CA502 |
| C | VAL262 |
| C | ASP263 |
| C | GLU264 |
| C | MET266 |
| C | ARG280 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | GLU264 |
| B | PG4501 |
| C | GLU264 |
| site_id | AC7 |
| Number of Residues | 38 |
| Details | binding site for residue FAD C 500 |
| Chain | Residue |
| B | TRP315 |
| B | ALA316 |
| C | GLY12 |
| C | GLY13 |
| C | GLY14 |
| C | PRO15 |
| C | ALA16 |
| C | LEU34 |
| C | ASP35 |
| C | LYS36 |
| C | ASN37 |
| C | GLY41 |
| C | ALA42 |
| C | LEU43 |
| C | THR46 |
| C | ILE49 |
| C | ASN51 |
| C | ALA82 |
| C | VAL84 |
| C | ALA111 |
| C | THR112 |
| C | GLY113 |
| C | GLY277 |
| C | ASP278 |
| C | LYS285 |
| C | GLN286 |
| C | ALA287 |
| C | ALA290 |
| C | HOH607 |
| C | HOH635 |
| C | HOH637 |
| C | HOH640 |
| C | HOH643 |
| C | HOH656 |
| C | HOH657 |
| C | HOH673 |
| C | HOH677 |
| B | ASP314 |
| site_id | AC8 |
| Number of Residues | 39 |
| Details | binding site for residue FAD D 401 |
| Chain | Residue |
| A | ASP314 |
| A | TRP315 |
| A | ALA316 |
| D | GLY12 |
| D | GLY13 |
| D | GLY14 |
| D | PRO15 |
| D | ALA16 |
| D | LEU34 |
| D | ASP35 |
| D | LYS36 |
| D | ASN37 |
| D | GLY41 |
| D | ALA42 |
| D | LEU43 |
| D | THR46 |
| D | ILE49 |
| D | ASN51 |
| D | ALA82 |
| D | VAL84 |
| D | ALA111 |
| D | THR112 |
| D | GLY113 |
| D | ILE244 |
| D | GLY277 |
| D | ASP278 |
| D | LYS285 |
| D | GLN286 |
| D | ALA287 |
| D | ALA290 |
| D | HOH604 |
| D | HOH630 |
| D | HOH642 |
| D | HOH649 |
| D | HOH651 |
| D | HOH653 |
| D | HOH672 |
| D | HOH675 |
| D | HOH679 |
