1l76: Difference between revisions

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[[Image:1l76.jpg|left|200px]]<br /><applet load="1l76" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1l76.jpg|left|200px]]
caption="1l76, resolution 1.9&Aring;" />
 
'''TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS'''<br />
{{Structure
|PDB= 1l76 |SIZE=350|CAPTION= <scene name='initialview01'>1l76</scene>, resolution 1.9&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=
}}
 
'''TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1L76 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1L76 OCA].  
1L76 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L76 OCA].  


==Reference==
==Reference==
Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions., Sauer UH, San DP, Matthews BW, J Biol Chem. 1992 Feb 5;267(4):2393-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1733941 1733941]
Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions., Sauer UH, San DP, Matthews BW, J Biol Chem. 1992 Feb 5;267(4):2393-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1733941 1733941]
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase (o-glycosyl)]]
[[Category: hydrolase (o-glycosyl)]]


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