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: 15321717DOI: 10.1016/J.JMB.2004.06.079 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report![Download](/newweb/media/icons/dl.png)
![Download](/newweb/media/icons/dl.png)