2HQM
Crystal Structure of Glutathione Reductase Glr1 from the Yeast Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005777 | cellular_component | peroxisome |
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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050661 | molecular_function | NADP binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005777 | cellular_component | peroxisome |
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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050661 | molecular_function | NADP binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
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 | GLY58-PRO68 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00390","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00390","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17554778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HQM","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P06715","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17554778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HQM","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | HIS472 | |
A | GLU477 | |
B | CYS61 | |
B | CYS66 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | CYS61 | |
A | CYS66 | |
B | HIS472 | |
B | GLU477 |