1KAH
L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINE (PRODUCT), ZN AND NAD (COFACTOR)
Summary for 1KAH
Entry DOI | 10.2210/pdb1kah/pdb |
Related | 1K75 1KAE 1KAR |
Descriptor | Histidinol dehydrogenase, ZINC ION, HISTIDINE (3 entities in total) |
Functional Keywords | l-histidinol dehydrogenase, homodimer, rossmann fold, 4 domains, hisd, l-histidine biosynthesis, nad cofactor, zinc, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 93405.96 |
Authors | Barbosa, J.A.R.G.,Sivaraman, J.,Li, Y.,Larocque, R.,Matte, A.,Schrag, J.D.,Cygler, M. (deposition date: 2001-11-02, release date: 2002-06-12, Last modification date: 2023-11-15) |
Primary citation | Barbosa, J.A.R.G.,Sivaraman, J.,Li, Y.,Larocque, R.,Matte, A.,Schrag, J.D.,Cygler, M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc.Natl.Acad.Sci.USA, 99:1859-1864, 2002 Cited by PubMed: 11842181DOI: 10.1073/pnas.022476199 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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