1K75
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
Summary for 1K75
| Entry DOI | 10.2210/pdb1k75/pdb |
| Descriptor | L-histidinol dehydrogenase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | l-histidinol dehydrogenase, homodimer, rossmann fold, 4 domains, hisd, l-histidine biosynthesis, nad cofactor, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 93345.39 |
| Authors | Barbosa, J.A.R.G.,Sivaraman, J.,Li, Y.,Larocque, R.,Matte, A.,Schrag, J.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2001-10-18, release date: 2002-02-27, Last modification date: 2014-11-12) |
| 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 (1.75 Å) |
Structure validation
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