1qal: Difference between revisions

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-[[Image:1qal.gif|left|200px]]<br /><applet load="1qal" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qal.gif|left|200px]]
-caption="1qal, resolution 2.2&Aring;" />
-'''THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS'''<br />
+ {{Structure
+|PDB= 1qal |SIZE=350|CAPTION= <scene name='initialview01'>1qal</scene>, resolution 2.2&Aring;
+|SITE=
+|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
+|ACTIVITY= [http://en.wikipedia.org/wiki/Amine_oxidase_(flavin-containing) Amine oxidase (flavin-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4]
+|GENE= MOAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+}}
+'''THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS'''
 ==Overview==
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 ==About this Structure==
-QAL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(flavin-containing) Amine oxidase (flavin-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAL OCA].
+QAL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAL OCA].
 ==Reference==
-The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants., Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ, Biochemistry. 1999 Jun 29;38(26):8217-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10387067 10387067]
+The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants., Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ, Biochemistry. 1999 Jun 29;38(26):8217-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10387067 10387067]
 [[Category: Amine oxidase (flavin-containing)]]
 [[Category: Escherichia coli]]
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 [[Category: mushroom shaped homodimer with mainly beta structure. there are 3 small peripheral alpha/beta domains.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:07 2008''