4GR1

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

Summary for 4GR1

• Entry DOI: 10.2210/pdb4gr1/pdb
• Descriptor: GLUTATHIONE REDUCTASE, PHOSPHATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: oxidoreductase (flavoenzyme)
• Biological source: Homo sapiens (human)
• Cellular location: Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic: Cytoplasm: P00390
• Total number of polymer chains: 1
• Total formula weight: 53129.39

Authors

Schulz, G.E.,Janes, W. (deposition date: 1990-03-26, release date: 1991-10-15, Last modification date: 2024-10-16)

Primary citation

Janes, W.,Schulz, G.E.
The binding of the retro-analogue of glutathione disulfide to glutathione reductase.
J.Biol.Chem., 265:10443-10445, 1990

PubMed 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.

PubMed: 2355009

Experimental method

X-RAY DIFFRACTION (2.4 Å)