1ijh: Difference between revisions

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[[Image:1ijh.gif|left|200px]]<br /><applet load="1ijh" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ijh.gif|left|200px]]
caption="1ijh, resolution 1.53&Aring;" />
 
'''CHOLESTEROL OXIDASE FROM STREPTOMYCES ASN485LEU MUTANT'''<br />
{{Structure
|PDB= 1ijh |SIZE=350|CAPTION= <scene name='initialview01'>1ijh</scene>, resolution 1.53&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6]
|GENE= choA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1931 Streptomyces sp.])
}}
 
'''CHOLESTEROL OXIDASE FROM STREPTOMYCES ASN485LEU MUTANT'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1IJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJH OCA].  
1IJH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJH OCA].  


==Reference==
==Reference==
The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase., Yin Y, Sampson NS, Vrielink A, Lario PI, Biochemistry. 2001 Nov 20;40(46):13779-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11705367 11705367]
The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase., Yin Y, Sampson NS, Vrielink A, Lario PI, Biochemistry. 2001 Nov 20;40(46):13779-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11705367 11705367]
[[Category: Cholesterol oxidase]]
[[Category: Cholesterol oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: steroid metabolism]]
[[Category: steroid metabolism]]


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