1GEU
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 | 36 |
Details | BINDING SITE FOR RESIDUE FAD A 451 |
Chain | Residue |
A | GLY11 |
A | CYS42 |
A | VAL45 |
A | GLY46 |
A | CYS47 |
A | LYS50 |
A | GLY113 |
A | PHE114 |
A | ALA115 |
A | ALA138 |
A | THR139 |
A | GLY13 |
A | GLY140 |
A | ARG263 |
A | ILE270 |
A | GLY302 |
A | ASP303 |
A | GLU309 |
A | LEU310 |
A | THR311 |
A | PRO312 |
A | NAD452 |
A | SER14 |
A | HOH467 |
A | HOH470 |
A | HOH477 |
A | HOH478 |
A | HOH515 |
B | HIS439 |
B | HOH497 |
A | GLY15 |
A | GLU34 |
A | ALA35 |
A | LYS36 |
A | GLY40 |
A | THR41 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD A 452 |
Chain | Residue |
A | GLY174 |
A | GLY176 |
A | TYR177 |
A | ILE178 |
A | GLU181 |
A | GLU197 |
A | MET198 |
A | PHE199 |
A | ALA229 |
A | PRO231 |
A | ALA260 |
A | ILE261 |
A | GLY262 |
A | GLU309 |
A | LEU310 |
A | VAL342 |
A | FAD451 |
A | HOH463 |
A | HOH493 |
A | HOH503 |
A | HOH514 |
A | HOH523 |
A | HOH546 |
A | HOH589 |
A | HOH600 |
site_id | AC3 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD B 451 |
Chain | Residue |
A | HIS439 |
A | PRO440 |
A | HOH458 |
A | HOH633 |
B | ILE10 |
B | GLY11 |
B | GLY13 |
B | SER14 |
B | GLY15 |
B | ILE33 |
B | GLU34 |
B | ALA35 |
B | GLY40 |
B | THR41 |
B | CYS42 |
B | GLY46 |
B | CYS47 |
B | LYS50 |
B | GLY113 |
B | PHE114 |
B | ALA115 |
B | ALA138 |
B | THR139 |
B | GLY140 |
B | ARG263 |
B | ILE270 |
B | GLY302 |
B | ASP303 |
B | GLU309 |
B | LEU310 |
B | THR311 |
B | PRO312 |
B | NAD452 |
B | HOH460 |
B | HOH466 |
B | HOH480 |
B | HOH508 |
B | HOH601 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD B 452 |
Chain | Residue |
B | VAL173 |
B | GLY174 |
B | GLY176 |
B | TYR177 |
B | ILE178 |
B | GLU181 |
B | GLU197 |
B | MET198 |
B | PHE199 |
B | PRO231 |
B | ALA260 |
B | ILE261 |
B | GLY262 |
B | GLU309 |
B | LEU310 |
B | THR341 |
B | VAL342 |
B | FAD451 |
B | HOH473 |
B | HOH495 |
B | HOH509 |
B | HOH517 |
B | HOH539 |
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 |