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 |
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 |