1cup: Difference between revisions

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[[Image:1cup.jpg|left|200px]]<br /><applet load="1cup" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1cup.jpg|left|200px]]
caption="1cup, resolution 1.89&Aring;" />
 
'''METHIONINE CORE MUTANT OF T4 LYSOZYME'''<br />
{{Structure
|PDB= 1cup |SIZE=350|CAPTION= <scene name='initialview01'>1cup</scene>, resolution 1.89&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=HED:2-HYDROXYETHYL DISULFIDE'>HED</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=
}}
 
'''METHIONINE CORE MUTANT OF T4 LYSOZYME'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1CUP 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=HED:'>HED</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=1CUP OCA].  
1CUP 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=1CUP OCA].  


==Reference==
==Reference==
Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding., Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW, Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545167 10545167]
Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding., Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW, Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10545167 10545167]
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: t4 lysozyme]]
[[Category: t4 lysozyme]]


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