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1SM9

Crystal Structure Of An Engineered K274RN276D Double Mutant of Xylose Reductase From Candida Tenuis Optimized To Utilize NAD

Summary for 1SM9
Entry DOI10.2210/pdb1sm9/pdb
Descriptorxylose reductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
Functional Keywordsxylose metabolism, coenzyme specificity, aldo-keto reductase, beta-alpha-barrel, akr2b5, oxidoreductase
Biological sourceCandida tenuis
Total number of polymer chains4
Total formula weight147018.50
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 citationPetschacher, 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: 15320875
DOI: 10.1042/BJ20040363
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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