1BDM

THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY

Summary for 1BDM

DescriptorMALATE DEHYDROGENASE, BETA-6-HYDROXY-1,4,5,6-TETRHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total)
Functional Keywordsoxidoreductase(nad(a)-choh(d))
Biological sourceThermus thermophilus
Total number of polymer chains2
Total molecular weight72296.4
Authors
Kelly, C.A.,Birktoft, J.J. (deposition date: 1993-02-16, release date: 1994-12-20, Last modification date: 2017-11-29)
Primary citation
Kelly, C.A.,Nishiyama, M.,Ohnishi, Y.,Beppu, T.,Birktoft, J.J.
Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
Biochemistry, 32:3913-3922, 1993
PubMed: 8471603 (PDB entries with the same primary citation)
DOI: 10.1021/bi00066a010
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers1207.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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