6B4O
1.73 Angstrom Resolution Crystal Structure of Glutathione Reductase from Enterococcus faecalis 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 43 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE9 |
| A | GLY39 |
| A | THR40 |
| A | CYS41 |
| A | GLY45 |
| A | CYS46 |
| A | LYS49 |
| A | GLY112 |
| A | TYR113 |
| A | ALA114 |
| A | ALA137 |
| A | GLY10 |
| A | THR138 |
| A | GLY139 |
| A | TYR176 |
| A | ARG262 |
| A | GLY301 |
| A | ASP302 |
| A | ASP308 |
| A | LEU309 |
| A | THR310 |
| A | PRO311 |
| A | GLY12 |
| A | HOH613 |
| A | HOH619 |
| A | HOH620 |
| A | HOH635 |
| A | HOH660 |
| A | HOH673 |
| A | HOH759 |
| A | HOH778 |
| A | HOH786 |
| A | HOH810 |
| A | SER13 |
| A | HOH823 |
| A | HOH877 |
| B | HIS438 |
| B | PRO439 |
| A | GLY14 |
| A | ILE32 |
| A | GLU33 |
| A | GLY34 |
| A | ASN35 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASP92 |
| A | HOH639 |
| A | HOH662 |
| A | HOH876 |
| A | HOH915 |
| A | HOH993 |
| A | HOH1006 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | HOH614 |
| A | HOH650 |
| A | HOH882 |
| A | HOH1093 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | ASN20 |
| A | ARG318 |
| A | HOH773 |
| A | HOH846 |
| A | HOH1009 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | ASP207 |
| A | GLU355 |
| A | LYS356 |
| A | HOH938 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 506 |
| Chain | Residue |
| A | GLY259 |
| A | GLY261 |
| A | HOH1012 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 507 |
| Chain | Residue |
| A | ALA174 |
| A | PHE196 |
| A | ARG197 |
| A | HOH1044 |
| A | HOH1070 |
| site_id | AC8 |
| Number of Residues | 42 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | ASP308 |
| B | LEU309 |
| B | THR310 |
| B | PRO311 |
| B | HOH607 |
| B | HOH628 |
| B | HOH631 |
| B | HOH642 |
| B | HOH704 |
| B | HOH722 |
| B | HOH727 |
| B | HOH743 |
| B | HOH771 |
| B | HOH928 |
| A | HIS438 |
| A | PRO439 |
| A | HOH791 |
| B | ILE9 |
| B | GLY10 |
| B | GLY12 |
| B | SER13 |
| B | GLY14 |
| B | ILE32 |
| B | GLU33 |
| B | GLY34 |
| B | ASN35 |
| B | GLY39 |
| B | THR40 |
| B | CYS41 |
| B | GLY45 |
| B | CYS46 |
| B | LYS49 |
| B | GLY112 |
| B | TYR113 |
| B | ALA114 |
| B | ALA137 |
| B | THR138 |
| B | GLY139 |
| B | TYR176 |
| B | ARG262 |
| B | GLY301 |
| B | ASP302 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASN28 |
| B | HOH688 |
| B | HOH959 |
| B | HOH1028 |
| C | HOH662 |
| C | HOH692 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | GLU150 |
| B | HOH960 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 504 |
| Chain | Residue |
| B | HOH732 |
| B | HOH754 |
| B | HOH822 |
| B | HOH1042 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 505 |
| Chain | Residue |
| B | HOH819 |
| B | HOH944 |
| B | HOH1029 |
| B | HOH1059 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | ASP207 |
| B | GLU355 |
| B | LYS356 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 507 |
| Chain | Residue |
| B | LEU202 |
| B | SER204 |
| B | HOH967 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 508 |
| Chain | Residue |
| B | GLY259 |
| B | GLY261 |
| B | HOH1000 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 509 |
| Chain | Residue |
| B | ASN20 |
| B | ARG318 |
| B | HOH737 |
| B | HOH1012 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 510 |
| Chain | Residue |
| B | ALA174 |
| B | ARG197 |
| B | HOH1036 |
| B | HOH1057 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 511 |
| Chain | Residue |
| B | HIS345 |
| B | PRO346 |
| B | HOH616 |
| B | HOH1112 |
| site_id | AE1 |
| Number of Residues | 42 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | ILE9 |
| C | GLY10 |
| C | GLY12 |
| C | SER13 |
| C | GLY14 |
| C | ILE32 |
| C | GLU33 |
| C | GLY34 |
| C | ASN35 |
| C | GLY39 |
| C | THR40 |
| C | CYS41 |
| C | GLY45 |
| C | CYS46 |
| C | LYS49 |
| C | GLY112 |
| C | TYR113 |
| C | ALA114 |
| C | ALA137 |
| C | THR138 |
| C | GLY139 |
| C | TYR176 |
| C | ILE177 |
| C | ARG262 |
| C | GLY301 |
| C | ASP302 |
| C | ASP308 |
| C | LEU309 |
| C | THR310 |
| C | PRO311 |
| C | HOH624 |
| C | HOH633 |
| C | HOH666 |
| C | HOH696 |
| C | HOH735 |
| C | HOH741 |
| C | HOH763 |
| C | HOH804 |
| C | HOH808 |
| D | HIS438 |
| D | PRO439 |
| D | HOH802 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | HOH606 |
| C | HOH746 |
| C | HOH781 |
| C | HOH926 |
| C | HOH953 |
| C | HOH959 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | ASN20 |
| C | ARG318 |
| C | HOH698 |
| C | HOH895 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 504 |
| Chain | Residue |
| C | ASP207 |
| C | GLU355 |
| C | LYS356 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 505 |
| Chain | Residue |
| C | GLY259 |
| C | GLY261 |
| C | HOH915 |
| C | HOH927 |
| site_id | AE6 |
| Number of Residues | 40 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS438 |
| C | PRO439 |
| D | ILE9 |
| D | GLY10 |
| D | GLY12 |
| D | SER13 |
| D | GLY14 |
| D | GLU33 |
| D | GLY34 |
| D | ASN35 |
| D | GLY39 |
| D | THR40 |
| D | CYS41 |
| D | GLY45 |
| D | CYS46 |
| D | LYS49 |
| D | GLY112 |
| D | TYR113 |
| D | ALA114 |
| D | ALA137 |
| D | THR138 |
| D | GLY139 |
| D | TYR176 |
| D | ARG262 |
| D | GLY301 |
| D | ASP302 |
| D | ASP308 |
| D | LEU309 |
| D | THR310 |
| D | PRO311 |
| D | HOH640 |
| D | HOH642 |
| D | HOH701 |
| D | HOH702 |
| D | HOH705 |
| D | HOH745 |
| D | HOH758 |
| D | HOH759 |
| D | HOH829 |
| D | HOH892 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | GLU150 |
| D | HOH961 |
| site_id | AE8 |
| Number of Residues | 1 |
| Details | binding site for residue MG D 503 |
| Chain | Residue |
| D | HOH818 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 504 |
| Chain | Residue |
| D | ASP92 |
| D | HOH605 |
| D | HOH628 |
| D | HOH884 |
| D | HOH950 |
| D | HOH984 |
| site_id | AF1 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 505 |
| Chain | Residue |
| A | HOH861 |
| A | HOH1083 |
| D | HOH698 |
| D | HOH748 |
| D | HOH1091 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 506 |
| Chain | Residue |
| D | ASP207 |
| D | GLU355 |
| D | LYS356 |
| D | HOH971 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 507 |
| Chain | Residue |
| D | LEU202 |
| D | ARG203 |
| D | SER204 |
| D | HOH927 |
| site_id | AF4 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 508 |
| Chain | Residue |
| D | ASN20 |
| D | ARG318 |
| D | HOH667 |
| D | HOH1007 |
| D | HOH1067 |
| site_id | AF5 |
| Number of Residues | 6 |
| Details | binding site for residue CL D 509 |
| Chain | Residue |
| D | ALA174 |
| D | PHE196 |
| D | ARG197 |
| D | HOH1024 |
| D | HOH1049 |
| D | HOH1070 |
| site_id | AF6 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 510 |
| Chain | Residue |
| D | GLY259 |
| D | GLY261 |
| D | HOH964 |
| D | HOH994 |
| site_id | AF7 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 511 |
| Chain | Residue |
| D | ASN265 |
| D | THR266 |
| D | ASP267 |
| D | GLN268 |
| site_id | AF8 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 512 |
| Chain | Residue |
| D | HIS111 |
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 | GLY38-PRO48 |
