6N7F
1.90 Angstrom Resolution Crystal Structure of Glutathione Reductase from Streptococcus pyogenes 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 | 41 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE10 |
| A | GLY40 |
| A | THR41 |
| A | CYS42 |
| A | GLY46 |
| A | CYS47 |
| A | LYS50 |
| A | TYR114 |
| A | ALA115 |
| A | ALA138 |
| A | THR139 |
| A | GLY11 |
| A | GLY140 |
| A | TYR177 |
| A | ARG263 |
| A | PHE270 |
| A | GLY302 |
| A | ASP303 |
| A | ALA309 |
| A | LEU310 |
| A | THR311 |
| A | PRO312 |
| A | GLY13 |
| A | HOH624 |
| A | HOH648 |
| A | HOH697 |
| A | HOH715 |
| A | HOH721 |
| A | HOH722 |
| A | HOH796 |
| A | HOH812 |
| A | HOH829 |
| B | HIS439 |
| A | SER14 |
| B | PRO440 |
| B | HOH697 |
| A | ALA15 |
| A | ALA33 |
| A | GLU34 |
| A | GLY35 |
| A | LYS36 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue RBF A 502 |
| Chain | Residue |
| A | GLY35 |
| A | LYS36 |
| A | TYR114 |
| A | HIS142 |
| A | ASN266 |
| A | GLU268 |
| A | GLY269 |
| A | HOH614 |
| A | HOH728 |
| A | HOH812 |
| A | HOH828 |
| A | HOH834 |
| A | HOH894 |
| A | HOH901 |
| A | HOH948 |
| D | GLY35 |
| D | LYS36 |
| D | TYR114 |
| D | HIS142 |
| D | ASN266 |
| D | GLU268 |
| D | GLY269 |
| D | HOH814 |
| D | HOH832 |
| D | HOH1025 |
| D | HOH1036 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue BTB A 503 |
| Chain | Residue |
| A | MET378 |
| A | HIS439 |
| A | PRO440 |
| A | THR441 |
| A | GLU444 |
| A | GLU445 |
| A | HOH750 |
| A | HOH817 |
| A | HOH919 |
| B | TYR91 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue BCT A 504 |
| Chain | Residue |
| A | ASN292 |
| A | THR330 |
| A | HOH888 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | ARG94 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 506 |
| Chain | Residue |
| A | ALA260 |
| A | GLY262 |
| A | HOH949 |
| A | HOH964 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 507 |
| Chain | Residue |
| A | ASN21 |
| A | ARG319 |
| A | HOH821 |
| A | HOH975 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 508 |
| Chain | Residue |
| A | ILE155 |
| A | SER156 |
| A | GLY159 |
| D | LYS274 |
| site_id | AC9 |
| Number of Residues | 40 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | ALA15 |
| B | ALA33 |
| B | GLU34 |
| B | GLY35 |
| B | LYS36 |
| B | GLY40 |
| B | THR41 |
| B | CYS42 |
| B | GLY46 |
| B | CYS47 |
| B | LYS50 |
| B | TYR114 |
| B | ALA115 |
| B | ALA138 |
| B | THR139 |
| B | GLY140 |
| B | TYR177 |
| B | ARG263 |
| B | PHE270 |
| B | GLY302 |
| B | ASP303 |
| B | ALA309 |
| B | LEU310 |
| B | THR311 |
| B | PRO312 |
| B | HOH613 |
| B | HOH634 |
| B | HOH638 |
| B | HOH642 |
| B | HOH658 |
| B | HOH663 |
| B | HOH671 |
| B | HOH672 |
| B | HOH801 |
| A | HIS439 |
| A | HOH755 |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | SER14 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue BTB B 502 |
| Chain | Residue |
| A | TYR91 |
| B | PHE375 |
| B | MET378 |
| B | HIS439 |
| B | PRO440 |
| B | THR441 |
| B | GLU444 |
| B | GLU445 |
| B | HOH734 |
| B | HOH806 |
| B | HOH871 |
| B | HOH888 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | ALA260 |
| B | GLY262 |
| B | HOH870 |
| B | HOH917 |
| B | HOH958 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | LEU203 |
| B | ARG204 |
| B | SER205 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | ASN21 |
| B | ARG319 |
| B | HOH681 |
| B | HOH942 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | ASP207 |
| B | LYS208 |
| B | GLU357 |
| B | HOH742 |
| site_id | AD6 |
| Number of Residues | 39 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | ILE10 |
| C | GLY11 |
| C | GLY13 |
| C | SER14 |
| C | ALA15 |
| C | GLU34 |
| C | GLY35 |
| C | LYS36 |
| C | GLY40 |
| C | THR41 |
| C | CYS42 |
| C | LEU45 |
| C | GLY46 |
| C | CYS47 |
| C | LYS50 |
| C | TYR114 |
| C | ALA115 |
| C | ALA138 |
| C | THR139 |
| C | GLY140 |
| C | TYR177 |
| C | ARG263 |
| C | PHE270 |
| C | GLY302 |
| C | ASP303 |
| C | ALA309 |
| C | LEU310 |
| C | THR311 |
| C | PRO312 |
| C | HOH606 |
| C | HOH617 |
| C | HOH620 |
| C | HOH665 |
| C | HOH691 |
| C | HOH719 |
| C | HOH731 |
| C | HOH762 |
| D | HIS439 |
| D | HOH702 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for residue BTB C 502 |
| Chain | Residue |
| C | PHE375 |
| C | MET378 |
| C | HIS439 |
| C | PRO440 |
| C | THR441 |
| C | GLU444 |
| C | GLU445 |
| C | HOH817 |
| C | HOH837 |
| C | HOH870 |
| D | TYR91 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | LEU203 |
| C | ARG204 |
| C | SER205 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 504 |
| Chain | Residue |
| C | ASP207 |
| C | LYS208 |
| C | GLU357 |
| C | HOH758 |
| C | HOH806 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 505 |
| Chain | Residue |
| C | ALA260 |
| C | GLY262 |
| C | HOH889 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 506 |
| Chain | Residue |
| C | ASN21 |
| C | ARG319 |
| C | HOH688 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 507 |
| Chain | Residue |
| C | LYS51 |
| C | TYR55 |
| D | BTB502 |
| site_id | AE4 |
| Number of Residues | 39 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS439 |
| C | PRO440 |
| C | HOH785 |
| D | ILE10 |
| D | GLY11 |
| D | GLY13 |
| D | SER14 |
| D | ALA15 |
| D | ALA33 |
| D | GLU34 |
| D | GLY35 |
| D | GLY40 |
| D | THR41 |
| D | CYS42 |
| D | GLY46 |
| D | CYS47 |
| D | LYS50 |
| D | TYR114 |
| D | ALA115 |
| D | ALA138 |
| D | THR139 |
| D | GLY140 |
| D | TYR177 |
| D | ARG263 |
| D | PHE270 |
| D | GLY302 |
| D | ASP303 |
| D | ALA309 |
| D | LEU310 |
| D | THR311 |
| D | PRO312 |
| D | HOH659 |
| D | HOH675 |
| D | HOH708 |
| D | HOH730 |
| D | HOH731 |
| D | HOH774 |
| D | HOH814 |
| D | HOH825 |
| site_id | AE5 |
| Number of Residues | 9 |
| Details | binding site for residue BTB D 502 |
| Chain | Residue |
| C | TYR91 |
| C | CL507 |
| D | MET378 |
| D | HIS439 |
| D | PRO440 |
| D | THR441 |
| D | GLU444 |
| D | GLU445 |
| D | HOH751 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 503 |
| Chain | Residue |
| D | ARG94 |
| D | HOH1029 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue CL D 504 |
| Chain | Residue |
| D | ALA260 |
| D | GLY262 |
| D | HOH908 |
| D | HOH924 |
| D | HOH939 |
| D | HOH954 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 505 |
| Chain | Residue |
| D | ASN21 |
| D | ARG319 |
| D | HOH943 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 506 |
| Chain | Residue |
| A | LYS274 |
| D | ILE155 |
| D | SER156 |
| D | GLY159 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 507 |
| Chain | Residue |
| D | GLU357 |
| D | VAL360 |
| D | HOH727 |
| D | HOH868 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnlGCVP |
| Chain | Residue | Details |
| A | GLY39-PRO49 |
