4gr1

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

spinqualitylabelsall models 4gr1, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Method: X-ray diffraction, Resolution 2.4Å Ligands: FAD, PO4, RGS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSHR_HUMAN Maintains high levels of reduced glutathione in the cytosol. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione Reductase

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