4gr1

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THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASETHE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE

Structural highlights

4gr1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Glutathione-disulfide reductase, with EC number 1.8.1.7
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

The binding of the retro-analogue of glutathione disulfide to glutathione reductase.,Janes W, Schulz GE J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Janes W, Schulz GE. The binding of the retro-analogue of glutathione disulfide to glutathione reductase. J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009

4gr1, resolution 2.40Å

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