This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

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1kar, resolution 2.10Å ()

Ligands:

,

Non-Standard Residues:

Gene:

HISD (Escherichia coli)

Activity:

Histidinol dehydrogenase, with EC number 1.1.1.23

Related:

1k75, 1kae, 1kah

Structural annotation:
Resources:	CATH : 1Kara02, 1Kara01, 1Karb01, 1Karb02 InterPro : Ipr012131, Ipr001692 Pfam : PF00815 SCOP : d1kara_, d1karb_ UniProt : P06988

Functional annotation:
Biological process:	histidine biosynthetic process amino acid biosynthetic process
Molecular function:	metal ion binding NAD binding histidinol dehydrogenase activity oxidoreductase activity zinc ion binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

L-Histidinol DehydrogenaseL-Histidinol Dehydrogenase

The enzyme l-histidinol dehydrogenase (HisD)

ALL INFORMATION IN HERE!!! sub-headings for topics of interest (mechanism, binding sites, etc.) Basic information, current knowledge of areas found, etc. Structural

Overall StructureOverall Structure

HisD is a homodimer, with each subunit consisting of a globule segment, and an extending tail. The two larger domains (1 and 2) are within the globule, and domains 3 and 4 are found in the tail. The cores of both domains (residues 124–236 in domain 1 & 237–381 in domain 2) adopt incomplete Rossmann folds, which lack the last strand-helix hairpin^[1]. To carry out its function, HisD relies on the presence of one Zn2+ cation per monomer, not for catalysis, but for substrate binding.

Enzymatic mechanismEnzymatic mechanism

Other information??Other information??

^[1]. ^[1].

ReferencesReferences

↑ ^1.0 ^1.1 ^1.2 Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:11842181 doi:10.1073/pnas.022476199

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Simon Loewen

[1kar-1] 1.0 ^1.1 ^1.2 Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:11842181 doi:10.1073/pnas.022476199

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