1GES
ANATOMY OF AN ENGINEERED NAD-BINDING SITE
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 | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A 451 |
| Chain | Residue |
| A | ILE10 |
| A | GLY40 |
| A | THR41 |
| A | CYS42 |
| A | GLY46 |
| A | CYS47 |
| A | LYS50 |
| A | GLY113 |
| A | PHE114 |
| A | ALA115 |
| A | ALA138 |
| A | GLY11 |
| A | THR139 |
| A | GLY140 |
| A | TYR177 |
| A | ARG263 |
| A | ILE270 |
| A | GLY302 |
| A | ASP303 |
| A | GLU309 |
| A | LEU310 |
| A | THR311 |
| A | GLY13 |
| A | PRO312 |
| A | HOH453 |
| A | HOH455 |
| A | HOH460 |
| A | HOH465 |
| A | HOH480 |
| A | HOH503 |
| A | HOH603 |
| B | HIS439 |
| B | PRO440 |
| A | SER14 |
| A | GLY15 |
| A | ILE33 |
| A | GLU34 |
| A | ALA35 |
| A | LYS36 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 451 |
| Chain | Residue |
| A | HIS439 |
| A | PRO440 |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| 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 | HOH458 |
| B | HOH465 |
| B | HOH466 |
| B | HOH513 |
| B | HOH524 |
| B | HOH581 |
| B | HOH651 |
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 |
| Chain | Residue | Details |
| A | HIS439 | |
| B | HIS439 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU34 | |
| B | GLU34 |
