1SM9
Crystal Structure Of An Engineered K274RN276D Double Mutant of Xylose Reductase From Candida Tenuis Optimized To Utilize NAD
Summary for 1SM9
Entry DOI | 10.2210/pdb1sm9/pdb |
Descriptor | xylose reductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
Functional Keywords | xylose metabolism, coenzyme specificity, aldo-keto reductase, beta-alpha-barrel, akr2b5, oxidoreductase |
Biological source | Candida tenuis |
Total number of polymer chains | 4 |
Total formula weight | 147018.50 |
Authors | Petschacher, B.,Leitgeb, S.,Kavanagh, K.L.,Wilson, D.K.,Nidetzky, B. (deposition date: 2004-03-08, release date: 2004-12-21, Last modification date: 2023-08-23) |
Primary citation | Petschacher, B.,Leitgeb, S.,Kavanagh, K.L.,Wilson, D.K.,Nidetzky, B. The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography. Biochem.J., 385:75-83, 2005 Cited by PubMed: 15320875DOI: 10.1042/BJ20040363 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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