1GER
THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016020 | cellular_component | membrane |
| 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 | 0071949 | molecular_function | FAD binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016020 | cellular_component | membrane |
| 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 | 0071949 | molecular_function | FAD 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 451 |
| Chain | Residue |
| A | ILE10 |
| A | CYS42 |
| A | GLY46 |
| A | CYS47 |
| A | LYS50 |
| A | GLY113 |
| A | PHE114 |
| A | ALA115 |
| A | ALA138 |
| A | THR139 |
| A | GLY140 |
| A | GLY11 |
| A | TYR177 |
| A | ARG263 |
| A | ILE270 |
| A | GLY302 |
| A | ASP303 |
| A | GLU309 |
| A | LEU310 |
| A | THR311 |
| A | PRO312 |
| A | HOH453 |
| A | GLY13 |
| A | HOH458 |
| A | HOH462 |
| A | HOH466 |
| A | HOH478 |
| A | HOH529 |
| A | HOH636 |
| B | HIS439 |
| B | PRO440 |
| A | SER14 |
| A | GLY15 |
| A | GLU34 |
| A | ALA35 |
| A | GLY40 |
| A | THR41 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 451 |
| Chain | Residue |
| A | HIS439 |
| A | PRO440 |
| A | HOH454 |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | ILE33 |
| B | GLU34 |
| B | ALA35 |
| B | LYS36 |
| B | GLY40 |
| B | THR41 |
| B | CYS42 |
| B | VAL45 |
| B | GLY46 |
| B | CYS47 |
| B | LYS50 |
| B | GLY113 |
| B | PHE114 |
| B | ALA115 |
| B | ALA138 |
| B | THR139 |
| B | GLY140 |
| B | TYR177 |
| B | ARG263 |
| B | ILE270 |
| B | GLY302 |
| B | ASP303 |
| B | GLU309 |
| B | LEU310 |
| B | THR311 |
| B | PRO312 |
| B | HOH452 |
| B | HOH453 |
| B | HOH462 |
| B | HOH463 |
| B | HOH560 |
| B | HOH596 |
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 | GLY39-PRO49 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00390 |
| Chain | Residue | Details |
| A | HIS439 | |
| B | HIS439 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00390 |
| Chain | Residue | Details |
| A | SER14 | |
| A | TYR99 | |
| A | ARG319 | |
| B | SER14 | |
| B | TYR99 | |
| B | ARG319 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7833810, ECO:0000269|PubMed:8061609, ECO:0007744|PDB:1GER, ECO:0007744|PDB:1GES, ECO:0007744|PDB:1GET, ECO:0007744|PDB:1GEU |
| Chain | Residue | Details |
| A | GLY15 | |
| B | GLY15 | |
| B | GLU34 | |
| B | THR41 | |
| B | CYS42 | |
| B | LYS50 | |
| B | ALA115 | |
| B | ASP303 | |
| B | THR311 | |
| B | HIS439 | |
| A | GLU34 | |
| A | THR41 | |
| A | CYS42 | |
| A | LYS50 | |
| A | ALA115 | |
| A | ASP303 | |
| A | THR311 | |
| A | HIS439 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7833810, ECO:0007744|PDB:1GET |
| Chain | Residue | Details |
| A | ALA175 | |
| B | ILE178 | |
| B | GLU181 | |
| B | ARG198 | |
| B | ARG204 | |
| B | GLY262 | |
| B | GLU309 | |
| B | VAL342 | |
| A | ILE178 | |
| A | GLU181 | |
| A | ARG198 | |
| A | ARG204 | |
| A | GLY262 | |
| A | GLU309 | |
| A | VAL342 | |
| B | ALA175 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | HIS439 | |
| A | GLU444 | |
| B | GLU181 | |
| B | CYS42 | |
| B | CYS47 | |
| B | TYR177 | |
| B | LYS50 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU181 | |
| A | CYS42 | |
| A | CYS47 | |
| A | TYR177 | |
| A | LYS50 | |
| B | HIS439 | |
| B | GLU444 |
