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2HQM

Crystal Structure of Glutathione Reductase Glr1 from the Yeast Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0098869biological_processcellular oxidant detoxification
B0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0034599biological_processcellular response to oxidative stress
B0045454biological_processcell redox homeostasis
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP
ChainResidueDetails
AGLY58-PRO68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00390","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00390","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17554778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HQM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P06715","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17554778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HQM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AHIS472
AGLU477
BCYS61
BCYS66

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS61
ACYS66
BHIS472
BGLU477

242500

PDB entries from 2025-10-01

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