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ANATOMY OF AN ENGINEERED NAD-BINDING SITE

Source organism: Escherichia coli
Biochemical function: FAD binding
Biological process: cellular oxidant detoxification
Cellular component: membrane

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EC 1.8.1.7: Glutathione-disulfide reductase

Reaction catalysed:
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Systematic name:
Glutathione:NADP(+) oxidoreductase
Alternative Name(s):
  • GSH reductase
  • GSSG reductase
  • Glutathione S-reductase
  • Glutathione reductase
  • Glutathione reductase (NADPH)
  • NADPH-GSSG reductase
  • NADPH-glutathione reductase
  • NADPH:oxidized-glutathione oxidoreductase

GO terms

Sequence families

Pfam Protein families (Pfam)
PF02852
Domain description: Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
Occurring in:
  1. Glutathione reductase
The deposited structure of PDB entry 1get contains 2 copies of Pfam domain PF02852 (Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain) in Glutathione reductase. Showing 1 copy in chain B.

PF00070
Domain description: Pyridine nucleotide-disulphide oxidoreductase
Occurring in:
  1. Glutathione reductase
The deposited structure of PDB entry 1get contains 2 copies of Pfam domain PF00070 (Pyridine nucleotide-disulphide oxidoreductase) in Glutathione reductase. Showing 1 copy in chain B.

InterPro InterPro annotations
IPR036188
Domain description: FAD/NAD(P)-binding domain superfamily
Occurring in:
  1. Glutathione reductase
IPR016156
Domain description: FAD/NAD-linked reductase, dimerisation domain superfamily
Occurring in:
  1. Glutathione reductase
IPR004099
Domain description: Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
Occurring in:
  1. Glutathione reductase
IPR012999
Domain description: Pyridine nucleotide-disulphide oxidoreductase, class I, active site
Occurring in:
  1. Glutathione reductase
IPR023753
Domain description: FAD/NAD(P)-binding domain
Occurring in:
  1. Glutathione reductase
IPR046952
Domain description: Glutathione reductase/thioredoxin reductase-like
Occurring in:
  1. Glutathione reductase
IPR006322
Domain description: Glutathione reductase, eukaryote/bacterial
Occurring in:
  1. Glutathione reductase
IPR001100
Domain description: Pyridine nucleotide-disulphide oxidoreductase, class I
Occurring in:
  1. Glutathione reductase

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
The deposited structure of PDB entry 1get contains 4 copies of CATH domain 3.50.50.60 (FAD/NAD(P)-binding domain) in Glutathione reductase. Showing 2 copies in chain B.
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
The deposited structure of PDB entry 1get contains 2 copies of CATH domain 3.30.390.30 (Enolase-like; domain 1) in Glutathione reductase. Showing 1 copy in chain B.
SCOP SCOP annotations
51943
Class: Alpha and beta proteins (a/b)
Fold: FAD/NAD(P)-binding domain
Superfamily: FAD/NAD(P)-binding domain
Occurring in:
  1. Glutathione reductase
The deposited structure of PDB entry 1get contains 4 copies of SCOP domain 51943 (FAD/NAD-linked reductases, N-terminal and central domains) in Glutathione reductase. Showing 2 copies in chain B.
55425
Class: Alpha and beta proteins (a+b)
Fold: CO dehydrogenase flavoprotein C-domain-like
Superfamily: FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Occurring in:
  1. Glutathione reductase
The deposited structure of PDB entry 1get contains 2 copies of SCOP domain 55425 (FAD/NAD-linked reductases, dimerisation (C-terminal) domain) in Glutathione reductase. Showing 1 copy in chain B.

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