5U1O
2.3 Angstrom Resolution Crystal Structure of Glutathione Reductase from Vibrio parahaemolyticus in Complex with FAD.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
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 | 0050661 | molecular_function | NADP binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
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 | 0050661 | molecular_function | NADP binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
C | 0005829 | cellular_component | cytosol |
C | 0006749 | biological_process | glutathione metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
C | 0034599 | biological_process | cellular response to oxidative stress |
C | 0045454 | biological_process | cell redox homeostasis |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0050661 | molecular_function | NADP binding |
C | 0098869 | biological_process | cellular oxidant detoxification |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
D | 0005829 | cellular_component | cytosol |
D | 0006749 | biological_process | glutathione metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
D | 0034599 | biological_process | cellular response to oxidative stress |
D | 0045454 | biological_process | cell redox homeostasis |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0050661 | molecular_function | NADP binding |
D | 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 501 |
Chain | Residue |
A | GLY15 |
A | CYS46 |
A | VAL49 |
A | GLY50 |
A | CYS51 |
A | LYS54 |
A | GLY117 |
A | PHE118 |
A | ALA119 |
A | ALA142 |
A | VAL143 |
A | GLY17 |
A | GLY144 |
A | TYR181 |
A | ILE182 |
A | ARG267 |
A | ILE274 |
A | GLY306 |
A | ASP307 |
A | GLU314 |
A | LEU315 |
A | THR316 |
A | SER18 |
A | PRO317 |
A | HOH651 |
A | HOH655 |
A | HOH656 |
A | HOH693 |
A | HOH735 |
B | HIS444 |
B | PRO445 |
A | GLY19 |
A | ILE37 |
A | GLU38 |
A | ALA39 |
A | GLY44 |
A | THR45 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | SER378 |
A | GLY379 |
A | GLU450 |
site_id | AC3 |
Number of Residues | 36 |
Details | binding site for residue FAD B 501 |
Chain | Residue |
A | HIS444 |
A | PRO445 |
B | GLY15 |
B | GLY17 |
B | SER18 |
B | GLY19 |
B | GLU38 |
B | ALA39 |
B | GLY44 |
B | THR45 |
B | CYS46 |
B | GLY50 |
B | CYS51 |
B | LYS54 |
B | GLY117 |
B | PHE118 |
B | ALA119 |
B | ALA142 |
B | VAL143 |
B | GLY144 |
B | TYR181 |
B | ILE182 |
B | ARG267 |
B | ILE274 |
B | GLY306 |
B | ASP307 |
B | GLU314 |
B | LEU315 |
B | THR316 |
B | PRO317 |
B | HOH655 |
B | HOH669 |
B | HOH671 |
B | HOH694 |
B | HOH715 |
B | HOH716 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | SER378 |
B | GLY379 |
B | GLU450 |
B | HOH739 |
site_id | AC5 |
Number of Residues | 38 |
Details | binding site for residue FAD C 501 |
Chain | Residue |
C | GLY144 |
C | TYR181 |
C | ILE182 |
C | ARG267 |
C | ILE274 |
C | GLY306 |
C | ASP307 |
C | GLU314 |
C | LEU315 |
C | THR316 |
C | PRO317 |
C | HOH623 |
C | HOH625 |
C | HOH640 |
C | HOH652 |
C | HOH664 |
C | HOH683 |
D | HIS444 |
D | PRO445 |
C | GLY15 |
C | GLY17 |
C | SER18 |
C | GLY19 |
C | GLU38 |
C | ALA39 |
C | ASP41 |
C | GLY44 |
C | THR45 |
C | CYS46 |
C | VAL49 |
C | GLY50 |
C | CYS51 |
C | LYS54 |
C | GLY117 |
C | PHE118 |
C | ALA119 |
C | ALA142 |
C | VAL143 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 502 |
Chain | Residue |
C | SER378 |
C | GLY379 |
C | GLU450 |
site_id | AC7 |
Number of Residues | 38 |
Details | binding site for residue FAD D 501 |
Chain | Residue |
C | HIS444 |
C | PRO445 |
D | GLY15 |
D | GLY17 |
D | SER18 |
D | GLY19 |
D | ILE37 |
D | GLU38 |
D | ALA39 |
D | ASP41 |
D | GLY44 |
D | THR45 |
D | CYS46 |
D | VAL49 |
D | GLY50 |
D | CYS51 |
D | LYS54 |
D | GLY117 |
D | PHE118 |
D | ALA119 |
D | ALA142 |
D | VAL143 |
D | GLY144 |
D | TYR181 |
D | ILE182 |
D | ARG267 |
D | ILE274 |
D | GLY306 |
D | ASP307 |
D | GLU314 |
D | LEU315 |
D | THR316 |
D | PRO317 |
D | HOH614 |
D | HOH654 |
D | HOH660 |
D | HOH669 |
D | HOH705 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue CL D 502 |
Chain | Residue |
D | LEU343 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 503 |
Chain | Residue |
D | SER378 |
D | GLY379 |
D | GLU450 |
D | HOH615 |
D | HOH742 |
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 | GLY43-PRO53 |