1yap: Difference between revisions

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[[Image:1yap.jpg|left|200px]]<br /><applet load="1yap" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1yap.jpg|left|200px]]
caption="1yap, resolution 1.8&Aring;" />
 
'''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS'''<br />
{{Structure
|PDB= 1yap |SIZE=350|CAPTION= <scene name='initialview01'>1yap</scene>, resolution 1.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
|GENE= HUMAN LYSOZYME WITH ILE 59 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1YAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YAP OCA].  
1YAP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YAP OCA].  


==Reference==
==Reference==
Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants., Takano K, Ogasahara K, Kaneda H, Yamagata Y, Fujii S, Kanaya E, Kikuchi M, Oobatake M, Yutani K, J Mol Biol. 1995 Nov 17;254(1):62-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7473760 7473760]
Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants., Takano K, Ogasahara K, Kaneda H, Yamagata Y, Fujii S, Kanaya E, Kikuchi M, Oobatake M, Yutani K, J Mol Biol. 1995 Nov 17;254(1):62-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7473760 7473760]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


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