1UXG

Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.

Summary for 1UXG

Entry DOI	10.2210/pdb1uxg/pdb
Related	1GUY 1UR5 1UXH 1UXI 1UXJ 1UXK
Descriptor	MALATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, FUMARIC ACID, ... (4 entities in total)
Functional Keywords	oxidoreductase, tricarboxylic acid cycle, malate dehydrogenase
Biological source	CHLOROFLEXUS AURANTIACUS
Total number of polymer chains	2
Total formula weight	67054.48
Authors	Bjork, A.,Dalhus, B.,Mantzilas, D.,Eijsink, V.G.H.,Sirevag, R. (deposition date: 2004-02-25, release date: 2004-08-26, Last modification date: 2023-12-13)
Primary citation	Bjork, A.,Dalhus, B.,Mantzilas, D.,Sirevag, R.,Eijsink, V.G.H. Large Improvement in the Thermal Stability of a Tetrameric Malate Dehydrogenase by Single Point Mutations at the Dimer-Dimer Interface. J.Mol.Biol., 341:1215-, 2004 Cited by PubMed: 15321717 DOI: 10.1016/J.JMB.2004.06.079 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation