Function and Biology

Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5

Source organism: Homo sapiens
Biochemical function: oxidoreductase activity
Biological process: cellular oxidant detoxification
Cellular component: extracellular exosome

EC 1.8.1.7: Glutathione-disulfide reductase

Reaction catalysed:
2 glutathione + NADP(+) = glutathione disulfide + NADPH.
Comments:
  • Activity is dependent on a redox-active disulfide in each of the active centers.
  • Formerly EC 1.6.4.2.
Systematic name:
Glutathione:NADP(+) oxidoreductase
Alternative Name(s):
  • GSH reductase
  • GSSG reductase
  • NADPH-GSSG reductase
  • NADPH-glutathione reductase
  • NADPH:oxidized-glutathione oxidoreductase
  • Glutathione S-reductase
  • Glutathione reductase
  • Glutathione reductase (NADPH)

Sequence families

Pfam Protein families (Pfam)
PF07992
Domain description: Pyridine nucleotide-disulphide oxidoreductase
Occurring in:
  1. Glutathione reductase, mitochondrial
1 copy of Pfam domain PF07992 (Pyridine nucleotide-disulphide oxidoreductase) in Glutathione reductase, mitochondrial in PDB 2gh5.

PF00070
Domain description: Pyridine nucleotide-disulphide oxidoreductase
Occurring in:
  1. Glutathione reductase, mitochondrial
1 copy of Pfam domain PF00070 (Pyridine nucleotide-disulphide oxidoreductase) in Glutathione reductase, mitochondrial in PDB 2gh5.

PF13738
Domain description: Pyridine nucleotide-disulphide oxidoreductase
Occurring in:
  1. Glutathione reductase, mitochondrial
1 copy of Pfam domain PF13738 (Pyridine nucleotide-disulphide oxidoreductase) in Glutathione reductase, mitochondrial in PDB 2gh5.

PF02852
Domain description: Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
Occurring in:
  1. Glutathione reductase, mitochondrial
1 copy of Pfam domain PF02852 (Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain) in Glutathione reductase, mitochondrial in PDB 2gh5.

InterPro InterPro annotations
IPR036188
Domain description: FAD/NAD(P)-binding domain superfamily
Occurring in:
  1. Glutathione reductase, mitochondrial
IPR006322
Domain description: Glutathione reductase, eukaryote/bacterial
Occurring in:
  1. Glutathione reductase, mitochondrial
IPR016156
Domain description: FAD/NAD-linked reductase, dimerisation domain superfamily
Occurring in:
  1. Glutathione reductase, mitochondrial
IPR012999
Domain description: Pyridine nucleotide-disulphide oxidoreductase, class I, active site
Occurring in:
  1. Glutathione reductase, mitochondrial
IPR004099
Domain description: Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
Occurring in:
  1. Glutathione reductase, mitochondrial
IPR023753
Domain description: FAD/NAD(P)-binding domain
Occurring in:
  1. Glutathione reductase, mitochondrial
IPR001100
Domain description: Pyridine nucleotide-disulphide oxidoreductase, class I
Occurring in:
  1. Glutathione reductase, mitochondrial

Structure domains

CATH CATH domains
3.50.50.60
Class: Alpha Beta
Architecture: 3-Layer(bba) Sandwich
Topology: FAD/NAD(P)-binding domain
Homology: FAD/NAD(P)-binding domain
Occurring in:
  1. Glutathione reductase, mitochondrial
2 copies of CATH domain 3.50.50.60 (FAD/NAD(P)-binding domain) in Glutathione reductase, mitochondrial in PDB 2gh5.
3.30.390.30
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Enolase-like; domain 1
Homology: Enolase-like; domain 1
Occurring in:
  1. Glutathione reductase, mitochondrial
1 copy of CATH domain 3.30.390.30 (Enolase-like; domain 1) in Glutathione reductase, mitochondrial in PDB 2gh5.