3f16: Difference between revisions

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 ==Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor (R)-N-(3-hydroxy-1-nitroso-1-oxopropan-2-yl)-4-methoxybenzenesulfonamide==
-<StructureSection load='3f16' size='340' side='right' caption='[[3f16]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
+<StructureSection load='3f16' size='340' side='right'caption='[[3f16]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3f16]] 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=3F16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F16 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3f16]] 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=3F16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F16 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=HS3:(2R)-3-HYDROXY-2-[(4-METHOXYPHENYL)SULFONYLAMINO]-N-OXO-PROPANAMIDE'>HS3</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]] 1.16&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f15|3f15]], [[3f17|3f17]], [[3f18|3f18]], [[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=HS3:(2R)-3-HYDROXY-2-[(4-METHOXYPHENYL)SULFONYLAMINO]-N-OXO-PROPANAMIDE'>HS3</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=3f16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f16 OCA], [https://pdbe.org/3f16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f16 RCSB], [https://www.ebi.ac.uk/pdbsum/3f16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f16 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=3f16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f16 OCA], [http://pdbe.org/3f16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f16 RCSB], [http://www.ebi.ac.uk/pdbsum/3f16 PDBsum]</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/f1/3f16_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/3f16_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 31: @@
 ==See Also==
-*[[Matrix metalloproteinase|Matrix metalloproteinase]]
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Macrophage elastase]]
+[[Category: Large Structures]]
-[[Category: Calderone, V]]
+[[Category: Calderone V]]
-[[Category: Elastase]]
-[[Category: Extracellular matrix]]
-[[Category: Glycoprotein]]
-[[Category: Hydrolase]]
-[[Category: Matrix metalloproteinase]]
-[[Category: Metal-binding]]
-[[Category: Metallo elastase]]
-[[Category: Metalloprotease]]
-[[Category: Mmp12]]
-[[Category: Protease]]
-[[Category: Secreted]]
-[[Category: Zymogen]]