3nx7: Difference between revisions

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 ==Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-Hydroxy-2-(N-(2-hydroxyethyl)4-methoxyphenylsulfonamido)acetamide==
-<StructureSection load='3nx7' size='340' side='right' caption='[[3nx7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='3nx7' size='340' side='right'caption='[[3nx7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nx7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NX7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nx7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NX7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NHK:N-HYDROXY-N~2~-(2-HYDROXYETHYL)-N~2~-[(4-METHOXYPHENYL)SULFONYL]GLYCINAMIDE'>NHK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f15|3f15]], [[3f16|3f16]], [[3f17|3f17]], [[3f19|3f19]], [[3f1a|3f1a]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NHK:N-HYDROXY-N~2~-(2-HYDROXYETHYL)-N~2~-[(4-METHOXYPHENYL)SULFONYL]GLYCINAMIDE'>NHK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HME, MMP12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nx7 OCA], [https://pdbe.org/3nx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nx7 RCSB], [https://www.ebi.ac.uk/pdbsum/3nx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nx7 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nx7 OCA], [http://pdbe.org/3nx7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nx7 RCSB], [http://www.ebi.ac.uk/pdbsum/3nx7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nx7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN]] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
+[https://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/3nx7_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/3nx7_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 29: @@
 </div>
 <div class="pdbe-citations 3nx7" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Macrophage elastase]]
+[[Category: Large Structures]]
-[[Category: Bertini, I]]
+[[Category: Bertini I]]
-[[Category: Calderone, V]]
+[[Category: Calderone V]]
-[[Category: Fragai, M]]
+[[Category: Fragai M]]
-[[Category: Giachetti, A]]
+[[Category: Giachetti A]]
-[[Category: Loconte, M]]
+[[Category: Loconte M]]
-[[Category: Luchinat, C]]
+[[Category: Luchinat C]]
-[[Category: Maletta, M]]
+[[Category: Maletta M]]
-[[Category: Nativi, C]]
+[[Category: Nativi C]]
-[[Category: Yeo, K J]]
+[[Category: Yeo KJ]]
-[[Category: Elastase]]
-[[Category: Hydrolase]]
-[[Category: Matrix metalloproteinase]]
-[[Category: Mmp12]]