1kae Summary

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

The structure was published by Barbosa, J.A.R.G., Sivaraman, J., Li, Y., et al., Matte, A., Schrag, J.D., and Cygler, M., in 2002 in a paper entitled "Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2001.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of Histidinol dehydrogenase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Histidinol dehydrogenase P06988 (1-434) (HISX_ECOLI)search Escherichia coli K-12search 100% 434 100%
B Histidinol dehydrogenase P06988 (1-434) (HISX_ECOLI)search Escherichia coli K-12search 100% 434 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P06988 (1 - 434) Histidinol dehydrogenase Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P06988) L-histidinol dehydrogenase HisDsearch Nitrogenase molybdenum iron protein domainsearch PF00815: Histidinol dehydrogenasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P06988) oxidoreductase activitysearch zinc ion bindingsearch histidinol dehydrogenase activitysearch NAD bindingsearch metal ion bindingsearch manganese ion bindingsearch histidine biosynthetic processsearch oxidation-reduction processsearch metabolic processsearch cellular amino acid biosynthetic processsearch

Chain InterPro annotation
A, B Histidinol dehydrogenase, conserved sitesearch Histidinol dehydrogenasesearch Aldehyde/histidinol dehydrogenasesearch Histidinol dehydrogenase, monofunctionalsearch