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Oxidoreductase (flavoenzyme) PDB id
4gr1
Jmol
Contents
Protein chain
461 a.a. *
Ligands
PO4
FAD
RGS
Waters ×514
* Residue conservation analysis
PDB id:
4gr1
Name: Oxidoreductase (flavoenzyme)
Title: The binding of the retro-analogue of glutathione disulfide t glutathione reductase
Structure: Glutathione reductase. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Biol. unit: Dimer (from PQS)
Resolution:
2.40Å     R-factor:   0.151    
Authors: G.E.Schulz,W.Janes
Key ref: W.Janes and G.E.Schulz (1990). The binding of the retro-analogue of glutathione disulfide to glutathione reductase. J Biol Chem, 265, 10443-10445. PubMed id: 2355009
Date:
26-Mar-90     Release date:   15-Oct-91    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00390  (GSHR_HUMAN) -  Glutathione reductase, mitochondrial
Seq:
Struc: 		 
Seq:
Struc: 		522 a.a.
461 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.8.1.7  - Glutathione-disulfide reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH
2 × glutathione
 + NADP(+)
 =
glutathione disulfide
Bound ligand (Het Group name = RGS)
matches with 48.15% similarity 		+ NADPH
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     soluble fraction   5 terms 
  Biological process     oxidation-reduction process   6 terms 
  Biochemical function     electron carrier activity     8 terms  

 

 
    reference    
 
 
J Biol Chem 265:10443-10445 (1990)
PubMed id: 2355009  
 
 
The binding of the retro-analogue of glutathione disulfide to glutathione reductase.
W.Janes, G.E.Schulz.
 
  ABSTRACT  
 
The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
9174360 V.S.Stoll, S.J.Simpson, R.L.Krauth-Siegel, C.T.Walsh, and E.F.Pai (1997).
Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
  Biochemistry, 36, 6437-6447.
PDB codes: 1grt 2grt 3grt 4grt 5grt
  7703850 E.V.Koonin, A.R.Mushegian, R.L.Tatusov, S.F.Altschul, S.H.Bryant, P.Bork, and A.Valencia (1994).
Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling.
  Protein Sci, 3, 2045-2054.  
8174559 K.J.Embrey, A.Mehta, S.J.Carrington, R.Jaouhari, J.H.McKie, and K.T.Douglas (1994).
Use of transferred nuclear-Overhauser-effect spectroscopy to measure the bound conformation of a disulphide-replaced analogue of glutathione disulphide as an inhibitor of yeast glutathione reductase.
  Eur J Biochem, 221, 793-799.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.