1cvk: Difference between revisions

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OCA

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-[[Image:1cvk.gif|left|200px]]<br /><applet load="1cvk" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cvk.gif|left|200px]]
-caption="1cvk, resolution 1.8&Aring;" />
-'''T4 LYSOZYME MUTANT L118A'''<br />
+ {{Structure
+|PDB= 1cvk |SIZE=350|CAPTION= <scene name='initialview01'>1cvk</scene>, resolution 1.8&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= GENE E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4])
+}}
+'''T4 LYSOZYME MUTANT L118A'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-CVK 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=1CVK OCA].
+CVK 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=1CVK OCA].
 ==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: Lysozyme]]
@@ Line 27: / Line 36: @@
 [[Category: t4 lysozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:26 2008''