4LA1
Crystal structure of SjTGR (thioredoxin glutathione reductase from Schistosoma japonicumi)complex with FAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | ILE113 |
| A | THR153 |
| A | CYS154 |
| A | VAL157 |
| A | GLY158 |
| A | CYS159 |
| A | LYS162 |
| A | ALA226 |
| A | ARG227 |
| A | GLY228 |
| A | ALA256 |
| A | GLY114 |
| A | THR257 |
| A | GLY258 |
| A | TYR296 |
| A | VAL297 |
| A | ARG393 |
| A | LEU400 |
| A | GLY432 |
| A | ASP433 |
| A | GLN440 |
| A | LEU441 |
| A | GLY115 |
| A | THR442 |
| A | PRO443 |
| A | HOH721 |
| A | HOH730 |
| A | HOH750 |
| A | HOH787 |
| A | HOH897 |
| A | HOH926 |
| B | HIS571 |
| B | PRO572 |
| A | GLY116 |
| B | HOH711 |
| A | SER117 |
| A | GLY118 |
| A | ASP137 |
| A | TYR138 |
| A | GLY152 |
| site_id | AC2 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FAD B 600 |
| Chain | Residue |
| A | HIS571 |
| A | PRO572 |
| A | HOH722 |
| B | GLY114 |
| B | GLY115 |
| B | GLY116 |
| B | SER117 |
| B | GLY118 |
| B | LEU136 |
| B | ASP137 |
| B | TYR138 |
| B | GLY152 |
| B | THR153 |
| B | CYS154 |
| B | VAL157 |
| B | GLY158 |
| B | CYS159 |
| B | LYS162 |
| B | ALA226 |
| B | ARG227 |
| B | GLY228 |
| B | ALA256 |
| B | THR257 |
| B | GLY258 |
| B | TYR296 |
| B | VAL297 |
| B | LYS300 |
| B | ARG393 |
| B | LEU400 |
| B | GLY432 |
| B | ASP433 |
| B | GLN440 |
| B | LEU441 |
| B | THR442 |
| B | PRO443 |
| B | HOH708 |
| B | HOH718 |
| B | HOH720 |
| B | HOH810 |
| B | HOH828 |
| B | HOH896 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP |
| Chain | Residue | Details |
| A | GLY151-PRO161 |
