2nnx: Difference between revisions

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OCA

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-[[Image:2nnx.gif|left|200px]]<br /><applet load="2nnx" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:2nnx.gif|left|200px]]
-caption="2nnx, resolution 2.30&Aring;" />
-'''Crystal Structure of the H46R, H48Q double mutant of human [Cu-Zn] Superoxide Dismutase'''<br />
+ {{Structure
+|PDB= 2nnx |SIZE=350|CAPTION= <scene name='initialview01'>2nnx</scene>, resolution 2.30&Aring;
+|SITE=
+|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
+|ACTIVITY= [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]
+|GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+}}
+'''Crystal Structure of the H46R, H48Q double mutant of human [Cu-Zn] Superoxide Dismutase'''
 ==Overview==
@@ Line 10: / Line 19: @@
 ==About this Structure==
-NNX 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=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNX OCA].
+NNX 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=2NNX OCA].
 ==Reference==
-Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability., Wang J, Caruano-Yzermans A, Rodriguez A, Scheurmann JP, Slunt HH, Cao X, Gitlin J, Hart PJ, Borchelt DR, J Biol Chem. 2007 Jan 5;282(1):345-52. Epub 2006 Nov 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17092942 17092942]
+Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability., Wang J, Caruano-Yzermans A, Rodriguez A, Scheurmann JP, Slunt HH, Cao X, Gitlin J, Hart PJ, Borchelt DR, J Biol Chem. 2007 Jan 5;282(1):345-52. Epub 2006 Nov 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17092942 17092942]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
@@ Line 24: / Line 33: @@
 [[Category: oxidoreductase; human; cu-zn superoxide dismutase; superoxide acceptor; familial amyotrophic lateral sclerosis mutant]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:48:47 2008''