1FEC
UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 1.7 ANGSTROM 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 | 41 |
Details | BINDING SITE FOR RESIDUE FAD A 499 |
Chain | Residue |
A | ILE9 |
A | ALA46 |
A | GLY49 |
A | THR50 |
A | CYS51 |
A | VAL54 |
A | GLY55 |
A | CYS56 |
A | LYS59 |
A | GLY124 |
A | GLY126 |
A | GLY10 |
A | ALA158 |
A | THR159 |
A | GLY160 |
A | TYR197 |
A | ILE198 |
A | ARG286 |
A | ARG289 |
A | LEU293 |
A | GLY325 |
A | ASP326 |
A | GLY12 |
A | MET332 |
A | LEU333 |
A | THR334 |
A | PRO335 |
A | ALA337 |
A | HOH515 |
A | HOH521 |
A | HOH523 |
A | HOH528 |
A | HOH584 |
A | SER13 |
A | HOH751 |
B | HIS460 |
A | GLY14 |
A | ILE33 |
A | ASP34 |
A | LEU35 |
A | ALA45 |
site_id | AC2 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD B 499 |
Chain | Residue |
A | HIS460 |
B | ILE9 |
B | GLY10 |
B | GLY12 |
B | SER13 |
B | GLY14 |
B | ILE33 |
B | ASP34 |
B | LEU35 |
B | ALA46 |
B | GLY49 |
B | THR50 |
B | CYS51 |
B | CYS56 |
B | LYS59 |
B | GLY124 |
B | GLY126 |
B | ALA158 |
B | THR159 |
B | GLY160 |
B | TYR197 |
B | ARG286 |
B | ARG289 |
B | LEU293 |
B | GLY325 |
B | ASP326 |
B | MET332 |
B | LEU333 |
B | THR334 |
B | PRO335 |
B | ALA337 |
B | HOH502 |
B | HOH505 |
B | HOH508 |
B | HOH515 |
B | HOH547 |
B | HOH798 |
B | HOH872 |
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 | GLY48-PRO58 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS460 | |
B | HIS460 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP34 | |
B | ASP34 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | GLU465 | |
A | HIS460 | |
B | CYS51 | |
B | GLU201 | |
B | CYS56 | |
B | TYR197 | |
B | LYS59 |
site_id | CSA2 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | CYS51 | |
A | GLU201 | |
A | CYS56 | |
A | LYS59 | |
A | TYR197 | |
B | GLU465 | |
B | HIS460 |