1GXF
CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE IN COMPLEX WITH THE INHIBITOR QUINACRINE MUSTARD
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 | 31 |
Details | BINDING SITE FOR RESIDUE FAD A 1492 |
Chain | Residue |
A | ILE11 |
A | GLY51 |
A | THR52 |
A | CYS53 |
A | VAL56 |
A | CYS58 |
A | LYS61 |
A | GLY126 |
A | GLY128 |
A | ALA160 |
A | SER161 |
A | GLY12 |
A | GLY162 |
A | ARG288 |
A | ARG291 |
A | GLY326 |
A | ASP327 |
A | MET333 |
A | LEU334 |
A | THR335 |
A | PRO336 |
A | HOH2022 |
A | GLY14 |
A | HOH2028 |
B | HIS461 |
A | SER15 |
A | GLY16 |
A | ASP36 |
A | VAL37 |
A | SER47 |
A | ALA48 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MAE A 1500 |
Chain | Residue |
A | TYR222 |
A | ARG223 |
A | ILE286 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE QUM A 1501 |
Chain | Residue |
A | LEU18 |
A | GLU19 |
A | TRP22 |
A | SER110 |
A | TYR111 |
A | GLU113 |
A | MET114 |
A | ASP117 |
A | QUM1502 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE QUM A 1502 |
Chain | Residue |
A | GLU19 |
A | CYS53 |
A | SER110 |
A | TYR111 |
A | ILE339 |
A | QUM1501 |
B | HIS461 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD B 1492 |
Chain | Residue |
A | HIS461 |
A | PRO462 |
B | ILE11 |
B | GLY12 |
B | GLY14 |
B | SER15 |
B | GLY16 |
B | ILE35 |
B | ASP36 |
B | VAL37 |
B | SER47 |
B | ALA48 |
B | GLY51 |
B | THR52 |
B | VAL56 |
B | GLY57 |
B | CYS58 |
B | LYS61 |
B | GLY126 |
B | GLY128 |
B | ALA160 |
B | SER161 |
B | GLY162 |
B | ARG288 |
B | ARG291 |
B | GLY326 |
B | ASP327 |
B | MET333 |
B | LEU334 |
B | THR335 |
B | PRO336 |
B | HOH2025 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE QUM B 1501 |
Chain | Residue |
B | LEU18 |
B | GLU19 |
B | TRP22 |
B | TYR111 |
B | GLU113 |
B | MET114 |
B | ASP117 |
B | QUM1502 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE QUM B 1502 |
Chain | Residue |
A | HIS461 |
B | GLU19 |
B | CYS53 |
B | SER110 |
B | TYR111 |
B | ILE339 |
B | QUM1501 |
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 | GLY50-PRO60 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | HIS461 | |
B | HIS461 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP36 | |
B | ASP36 |
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 | PHE199 | |
B | CYS58 | |
B | LYS61 | |
B | CYS53 | |
B | GLU203 |
site_id | CSA2 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | LYS61 | |
A | PHE199 | |
A | CYS58 | |
A | CYS53 | |
A | GLU203 | |
B | GLU466 | |
B | HIS461 |