3GX0
Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase
Summary for 3GX0
Entry DOI | 10.2210/pdb3gx0/pdb |
Descriptor | GST-like protein yfcG, OXIDIZED GLUTATHIONE DISULFIDE (3 entities in total) |
Functional Keywords | transferase, glutathione, glutathione disulfide, disulfide bond oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 25158.49 |
Authors | Ladner, J.E.,Harp, J.M.,Wadington, M.C.,Armstrong, R.N. (deposition date: 2009-04-01, release date: 2009-07-07, Last modification date: 2024-02-21) |
Primary citation | Wadington, M.C.,Ladner, J.E.,Stourman, N.V.,Harp, J.M.,Armstrong, R.N. Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase. Biochemistry, 48:6559-6561, 2009 Cited by PubMed: 19537707DOI: 10.1021/bi9008825 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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