Revision as of 00:51, 3 April 2011

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

My Protein of Interest (MPI)My Protein of Interest (MPI)

Basic information, current knowledge of areas found, etc.

PicturePicture

Sec structure ^[1].

^[1].

StructureStructure

disulphides, secondary, etc. ^[2]

FunctionFunction

evolutionary purpose?

ReferencesReferences

↑ ^1.0 ^1.1 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
↑ Fallone CA. Epidemiology of the antibiotic resistance of Helicobacter pylori in Canada. Can J Gastroenterol. 2000 Nov;14(10):879-82. PMID:11111111

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 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

[supersecondary-2] Fallone CA. Epidemiology of the antibiotic resistance of Helicobacter pylori in Canada. Can J Gastroenterol. 2000 Nov;14(10):879-82. PMID:11111111

[1]

[2]

@@ Line 12: / Line 12: @@
 ==Structure==
 disulphides, secondary, etc.
-<ref name="superseconday"> PMID: </ref>
+<ref name="supersecondary"> PMID:11111111 </ref>

Sandbox Reserved 328: Difference between revisions

Revision as of 00:51, 3 April 2011

Contents

My Protein of Interest (MPI)My Protein of Interest (MPI)

PicturePicture

StructureStructure

FunctionFunction

ReferencesReferences

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Sandbox Reserved 328: Difference between revisions

Revision as of 00:51, 3 April 2011

My Protein of Interest (MPI)My Protein of Interest (MPI)

PicturePicture

StructureStructure

FunctionFunction

ReferencesReferences

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