1TYP
SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM 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 | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A 493 |
| Chain | Residue |
| A | ILE10 |
| A | GLY50 |
| A | THR51 |
| A | CYS52 |
| A | GLY56 |
| A | CYS57 |
| A | LYS60 |
| A | GLY125 |
| A | TRP126 |
| A | GLY127 |
| A | ALA159 |
| A | GLY11 |
| A | THR160 |
| A | GLY161 |
| A | TYR198 |
| A | ARG287 |
| A | LEU294 |
| A | GLY326 |
| A | ASP327 |
| A | MET333 |
| A | LEU334 |
| A | THR335 |
| A | GLY13 |
| A | PRO336 |
| A | HOH501 |
| A | HOH503 |
| A | HOH516 |
| A | HOH540 |
| A | HOH621 |
| B | HIS461 |
| B | PRO462 |
| A | SER14 |
| A | GLY15 |
| A | ASP35 |
| A | LEU36 |
| A | ALA46 |
| A | ALA47 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP A 494 |
| Chain | Residue |
| A | GLY195 |
| A | GLY196 |
| A | GLY197 |
| A | TYR198 |
| A | TYR221 |
| A | ARG222 |
| A | ARG228 |
| A | PHE230 |
| A | ILE285 |
| A | GLY286 |
| A | ARG287 |
| A | MET333 |
| A | CYS364 |
| A | VAL366 |
| A | HOH634 |
| A | HOH660 |
| A | HOH661 |
| A | HOH668 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GSH A 495 |
| Chain | Residue |
| A | SER14 |
| A | VAL58 |
| A | TYR110 |
| A | THR335 |
| A | ILE339 |
| A | SPD496 |
| A | GSH497 |
| A | HOH537 |
| A | HOH633 |
| A | HOH635 |
| A | HOH636 |
| B | HIS461 |
| B | GLU467 |
| B | SER470 |
| B | HOH633 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SPD A 496 |
| Chain | Residue |
| A | LEU17 |
| A | GLU18 |
| A | TRP21 |
| A | MET113 |
| A | GSH495 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GSH A 497 |
| Chain | Residue |
| A | LYS61 |
| A | ILE106 |
| A | TYR110 |
| A | GSH495 |
| A | SPD498 |
| B | HIS461 |
| B | PRO462 |
| B | THR463 |
| B | GLU466 |
| B | GLU467 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SPD A 498 |
| Chain | Residue |
| A | SER109 |
| A | GSH497 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD B 493 |
| Chain | Residue |
| B | GLY56 |
| B | CYS57 |
| B | LYS60 |
| B | GLY125 |
| B | TRP126 |
| B | GLY127 |
| B | ALA159 |
| B | THR160 |
| B | GLY161 |
| B | TYR198 |
| B | ARG287 |
| B | ARG290 |
| B | LEU294 |
| B | GLY326 |
| B | ASP327 |
| B | MET333 |
| B | LEU334 |
| B | THR335 |
| B | PRO336 |
| B | NAP494 |
| B | HOH501 |
| B | HOH502 |
| B | HOH505 |
| B | HOH508 |
| B | HOH535 |
| A | HIS461 |
| B | GLY11 |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | ASP35 |
| B | ALA46 |
| B | ALA47 |
| B | GLY50 |
| B | THR51 |
| B | CYS52 |
| B | VAL55 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP B 494 |
| Chain | Residue |
| B | LEU167 |
| B | GLY195 |
| B | GLY196 |
| B | GLY197 |
| B | TYR198 |
| B | ILE199 |
| B | TYR221 |
| B | ARG222 |
| B | ARG228 |
| B | PHE230 |
| B | ILE285 |
| B | GLY286 |
| B | ARG287 |
| B | MET333 |
| B | LEU334 |
| B | CYS364 |
| B | ALA365 |
| B | FAD493 |
| B | HOH628 |
| B | HOH631 |
| B | HOH655 |
| B | HOH665 |
| B | HOH671 |
| B | HOH696 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GSH B 495 |
| Chain | Residue |
| A | HIS461 |
| A | SER470 |
| B | SER14 |
| B | GLU18 |
| B | TYR110 |
| B | THR335 |
| B | ILE339 |
| B | SPD496 |
| B | GSH497 |
| B | HOH667 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SPD B 496 |
| Chain | Residue |
| B | LEU17 |
| B | GLU18 |
| B | TRP21 |
| B | MET113 |
| B | GSH495 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GSH B 497 |
| Chain | Residue |
| A | PHE396 |
| A | HIS461 |
| A | PRO462 |
| A | THR463 |
| A | SER464 |
| B | ILE106 |
| B | TYR110 |
| B | GSH495 |
| B | SPD498 |
| B | HOH677 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SPD B 498 |
| Chain | Residue |
| B | SER109 |
| B | GLY112 |
| B | GSH497 |
| B | HOH692 |
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 | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS461 | |
| B | HIS461 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP35 | |
| B | ASP35 |
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 |
