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PDBe Entry: 1bdm view

THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY
Summary
Header OXIDOREDUCTASE(NAD(A)-CHOH(D))search
Method X-RAY DIFFRACTION
Experiment Resolution: 1.8 Å, R-factor: 16.9%, Spacegroup: P 21 21 21
Released 20/12/1994, deposition: 16/02/1993, last revision: 24/02/2009
Authors Kelly, C.A.search; Birktoft, J.J.search
Primary citation Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
BIOCHEMISTRYsearch vol:32, pag:3913-3922 (1993) [PubMed ID 8471603 ]search
Keywords OXIDOREDUCTASE(NAD(A)-CHOH(D))search
EC 1.1.1.37 ExPASy BRENDA search (A B)
Organism Thermus thermophilus 274search(A B)
UniProt Malate dehydrogenase (EC 1.1.1.37) P10584search (A B)
Solvent A, B
Polymers
Id Name Type UniProt Residues Observed
A, B MALATE DEHYDROGENASE Protein P10584 (MDH_THETH)search
327 100%
Heterogens
Id Name Ligands
A, B BETA-6-HYDROXY-1,4,5,6-TETRHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE NAX search
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