2R9Z
Glutathione amide reductase from Chromatium gracile
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A 500 |
| Chain | Residue |
| A | GLY11 |
| A | CYS42 |
| A | VAL45 |
| A | GLY46 |
| A | CYS47 |
| A | LYS50 |
| A | GLY112 |
| A | HIS113 |
| A | ALA114 |
| A | ALA137 |
| A | THR138 |
| A | GLY13 |
| A | GLY139 |
| A | TYR176 |
| A | ARG262 |
| A | LEU269 |
| A | GLY301 |
| A | ASP302 |
| A | GLN308 |
| A | LEU309 |
| A | THR310 |
| A | PRO311 |
| A | SER14 |
| A | HOH501 |
| A | HOH505 |
| A | HOH508 |
| A | HOH537 |
| A | HOH658 |
| A | HOH693 |
| B | HIS437 |
| B | PRO438 |
| A | GLY15 |
| A | GLU34 |
| A | SER35 |
| A | LYS36 |
| A | GLY40 |
| A | THR41 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 464 |
| Chain | Residue |
| A | ARG104 |
| B | SER280 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 466 |
| Chain | Residue |
| A | HIS120 |
| A | HIS383 |
| A | HOH699 |
| A | HOH744 |
| A | HOH745 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A 468 |
| Chain | Residue |
| A | THR2 |
| A | GLN3 |
| A | HIS4 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 469 |
| Chain | Residue |
| A | HIS58 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD B 500 |
| Chain | Residue |
| A | HIS437 |
| A | PRO438 |
| B | GLY11 |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | GLU34 |
| B | SER35 |
| B | LYS36 |
| B | GLY40 |
| B | THR41 |
| B | CYS42 |
| B | VAL45 |
| B | GLY46 |
| B | CYS47 |
| B | LYS50 |
| B | GLY112 |
| B | HIS113 |
| B | ALA114 |
| B | ALA137 |
| B | THR138 |
| B | GLY139 |
| B | ILE177 |
| B | ARG262 |
| B | GLY301 |
| B | ASP302 |
| B | GLN308 |
| B | LEU309 |
| B | THR310 |
| B | PRO311 |
| B | HOH526 |
| B | HOH597 |
| B | HOH636 |
| B | HOH644 |
| B | HOH645 |
| B | HOH674 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 464 |
| Chain | Residue |
| A | SER280 |
| B | ARG104 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 465 |
| Chain | Residue |
| B | ARG115 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 466 |
| Chain | Residue |
| B | HIS120 |
| B | HIS383 |
| B | HOH696 |
| B | HOH697 |
| B | HOH698 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 467 |
| Chain | Residue |
| B | ARG267 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI B 468 |
| Chain | Residue |
| B | THR2 |
| B | GLN3 |
| B | HIS4 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 469 |
| Chain | Residue |
| B | HIS58 |
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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17977556","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17977556","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS42 | |
| A | CYS47 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS42 | |
| B | CYS47 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | HIS437 | |
| A | GLU442 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | HIS437 | |
| B | GLU442 |
