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1KAE

L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINOL (SUBSTRATE), ZINC AND NAD (COFACTOR)

Summary for 1KAE
Entry DOI10.2210/pdb1kae/pdb
Related1K75 1KAH 1KAR
DescriptorHistidinol dehydrogenase, SULFATE ION, ZINC ION, ... (9 entities in total)
Functional Keywordsl-histidinol dehydrogenase, homodimer, rossmann fold, 4 domains, hisd, l-histidine biosynthesis, nad cofactor, oxidoreductase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight95262.35
Authors
Barbosa, J.A.R.G.,Sivaraman, J.,Li, Y.,Larocque, R.,Matte, A.,Schrag, J.D.,Cygler, M. (deposition date: 2001-11-01, release date: 2002-06-12, Last modification date: 2023-11-15)
Primary citationBarbosa, 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: 11842181
DOI: 10.1073/pnas.022476199
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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