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BRENDA support

Literature summary extracted from

  • Li, X.Y.; Zhang, J.C.; Zhu, Y.Y.; Su, J.G.
    Domain motions and functionally-key residues of L-alanine dehydrogenase revealed by an elastic network model (2015), Int. J. Mol. Sci., 16, 29383-29397 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.1.1 investigation of functional domain motions by using the Gaussian network model and the anisotropy network model. The domain motions have a common hinge axis centered in residues Met133 and Met301. Both the NAD-binding domain and the substrate-binding domain move in a highly coupled way. The first three slowest modes exhibit the open-closed, rotation and twist motions Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.1 Mycobacterium tuberculosis P9WQB1
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1.4.1.1 Mycobacterium tuberculosis H37Rv P9WQB1
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