1TYT
CRYSTAL AND MOLECULAR STRUCTURE OF CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.6 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0015042 | molecular_function | trypanothione-disulfide reductase (NADPH) activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0015042 | molecular_function | trypanothione-disulfide reductase (NADPH) activity |
| 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 | 34 |
| Details | BINDING SITE FOR RESIDUE FAD A 493 |
| Chain | Residue |
| A | ILE10 |
| A | THR51 |
| A | CYS52 |
| A | VAL55 |
| A | CYS57 |
| A | LYS60 |
| A | GLY127 |
| A | ALA159 |
| A | THR160 |
| A | GLY161 |
| A | TYR198 |
| A | GLY11 |
| A | ARG287 |
| A | ARG290 |
| A | GLY326 |
| A | ASP327 |
| A | MET333 |
| A | LEU334 |
| A | THR335 |
| A | PRO336 |
| A | ALA338 |
| A | HOH498 |
| A | GLY13 |
| A | HOH510 |
| A | HOH534 |
| A | HOH639 |
| B | HIS461 |
| B | PRO462 |
| A | SER14 |
| A | GLY15 |
| A | ASP35 |
| A | ALA46 |
| A | ALA47 |
| A | GLY50 |
| site_id | AC2 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD B 493 |
| Chain | Residue |
| A | HIS461 |
| A | PRO462 |
| B | GLY11 |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | ASP35 |
| B | LEU36 |
| B | ALA46 |
| B | ALA47 |
| B | GLY50 |
| B | THR51 |
| B | CYS52 |
| B | VAL55 |
| B | CYS57 |
| B | LYS60 |
| B | GLY125 |
| B | PHE126 |
| B | GLY127 |
| B | THR160 |
| B | GLY161 |
| B | SER178 |
| B | TYR198 |
| B | ARG287 |
| B | ARG290 |
| B | THR293 |
| B | LEU294 |
| B | GLY326 |
| B | ASP327 |
| B | MET333 |
| B | LEU334 |
| B | THR335 |
| B | PRO336 |
| B | HOH497 |
| B | HOH500 |
| B | HOH504 |
| B | HOH507 |
| B | HOH540 |
| B | HOH622 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP |
| Chain | Residue | Details |
| A | GLY49-PRO59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU466 | |
| A | HIS461 | |
| B | TYR198 | |
| B | LYS60 | |
| B | CYS52 | |
| B | CYS57 | |
| B | GLU202 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | LYS60 | |
| A | TYR198 | |
| A | CYS52 | |
| A | CYS57 | |
| A | GLU202 | |
| B | GLU466 | |
| B | HIS461 |
