_EC 1.8.1.7 Glutathione-disulfide reductase. 34 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,663 PDB entries]
EC 1.8.-.- Acting on a sulfur group of donors. [334 PDB entries]
EC 1.8.1.- With NAD(+) or NADP(+) as acceptor. [192 PDB entries]
EC 1.8.1.7 Glutathione-disulfide reductase. [34 PDB entries]    
1alg

Reaction: 2 glutathione + NADP(+) = glutathione disulfide + Nadph.
 


2 × glutathione
+
NADP(+)
=
glutathione disulfide
+
NADPH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Glutathione reductase. Glutathione reductase (NADPH). Glutathione S-reductase. Gsh reductase. Gssg reductase. NADPH-glutathione reductase. NADPH-Gssg reductase. NADPH:oxidized-glutathione oxidoreductase.
Cofactor(s): Fad.
 

FAD
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: Activity is dependent on a redox-active disulfide in each of the active centers. Formerly Ec 1.6.4.2.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 34 PDB entries in enzyme class E.C.1.8.1.7

  PDB code Protein
1alg
Solution structure of an hgr inhibitor, nmr, 10 structures
Source: Synthetic construct. Organism_taxid: 32630
Chain: A (24 residues)
1bwc
Structure of human glutathione reductase complexed with ajoe inhibitor and subversive substrate
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell: erythrocytes. Gene: gor. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1dnc
Human glutathione reductase modified by diglutathione-dinitr
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
1ger
The structure of glutathione reductase from escherichia coli at 1.86 angstroms resolution: comparison with the enzyme from human erythrocytes
Source: Escherichia coli. Organism_taxid: 562
Chains: A, B (448 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1ges
Anatomy of an engineered NAD-binding site
Source: Escherichia coli. Organism_taxid: 562
Chains: A, B (448 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1get
Anatomy of an engineered NAD-binding site
Source: Escherichia coli. Organism_taxid: 562
Chains: A, B (448 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group NAP corresponds to enzyme reactant NADP(+)
  Het Group FAD corresponds to enzyme cofactor FAD
1geu
Anatomy of an engineered NAD-binding site
Source: Escherichia coli. Organism_taxid: 562
Chains: A, B (448 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group NAD is 91.00% similar to enzyme reactant NADP(+)
  Het Group FAD corresponds to enzyme cofactor FAD
1gra
Substrate binding and catalysis by glutathione reductase as from refined enzyme: substrate crystal structures at 2 angs resolution
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
1grb
Substrate binding and catalysis by glutathione reductase as from refined enzyme: substrate crystal structures at 2 angs resolution
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group NDP corresponds to enzyme reactant NADP(+)
  Het Group FAD corresponds to enzyme cofactor FAD
1gre
Substrate binding and catalysis by glutathione reductase as from refined enzyme: substrate crystal structures at 2 angs resolution
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
1grf
Substrate binding and catalysis by glutathione reductase as from refined enzyme: substrate crystal structures at 2 angs resolution
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1grg
Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 angstroms resolution
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1grh
Inhibition of human glutathione reductase by the nitrosourea 3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3- hydroxyethyl)-1-nitrosourea
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
1grt
Human glutathione reductase a34e/r37w mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Cell: red blood cell. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (462 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1gsn
Human glutathione reductase modified by dinitrosoglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
1k4q
Human glutathione reductase inactivated by peroxynitrite
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (463 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1onf
Crystal structure of plasmodium falciparum glutathione reduc
Source: Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Gene: gr2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (439 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD is 98.11% similar to enzyme cofactor FAD
1xan
Human glutathione reductase in complex with a xanthene inhib
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2aaq
Crystal structure analysis of the human glutahione reductase complexed with gopi
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hgr. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2gh5
Crystal structure of human glutathione reductase complexed w fluoro-analogue of the menadione derivative m5
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsr, glur, grd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2grt
Human glutathione reductase a34e, r37w mutant, oxidized glut complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Cell: red blood cells. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GDS corresponds to enzyme product glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
2hqm
Crystal structure of glutathione reductase glr1 from the yea saccharomyces cerevisiae
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
3djg
Catalytic cycle of human glutathione reductase near 1 a reso
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsr, glur, grd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: X (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group NDP corresponds to enzyme reactant NADP(+)
  Het Group FAD corresponds to enzyme cofactor FAD
3djj
Catalytic cycle of human glutathione reductase near 1 a reso
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsr, glur, grd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (462 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group NDP corresponds to enzyme reactant NADP(+)
  Het Group FAD corresponds to enzyme cofactor FAD
3dk4
Catalytic cycle of human glutathione reductase near 1 a reso
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsr, glur, grd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (462 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group NDP corresponds to enzyme reactant NADP(+)
  Het Group FAD corresponds to enzyme cofactor FAD
3dk8
Catalytic cycle of human glutathione reductase near 1 a reso
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsr, glur, grd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (462 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group GSH corresponds to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
3dk9
Catalytic cycle of human glutathione reductase near 1 a reso
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsr, glur, grd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (462 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
3grs
Refined structure of glutathione reductase at 1.54 angstroms resolution
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
3grt
Human glutathione reductase a34e, r37w mutant, oxidized tryp complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Cell: red blood cells. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group TS2 is 76.00% similar to enzyme product glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
3sqp
Structure of human glutathione reductase complexed with pyoc agent with antimalarial activity
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group 3J8 is 50.00% similar to enzyme reactant glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
4dna
Crystal structure of putative glutathione reductase from sin meliloti 1021
Source: Sinorhizobium meliloti. Ensifer meliloti. Organism_taxid: 266834. Strain: 1021. Gene: cac46433.1, gor, r01854, smc00154. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
4gr1
The binding of the retro-analogue of glutathione disulfide t glutathione reductase
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group RGS is 48.15% similar to enzyme product glutathione
  Het Group FAD corresponds to enzyme cofactor FAD
4grt
Human glutathione reductase a34e, r37w mutant, mixed disulfi trypanothione and the enzyme
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Cell: red blood cells. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
5grt
Human glutathione reductase a34e, r37w mutant, glutathionyls complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Cell: red blood cells. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (461 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
Bound ligands:   Het Group TS4 is 63.33% similar to enzyme product glutathione
  Het Group FAD corresponds to enzyme cofactor FAD