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1os2
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1os2.png|left|200px]] | ||
| - | + | ==Ternary enzyme-product-inhibitor complexes of human MMP12== | |
| - | + | <StructureSection load='1os2' size='340' side='right'caption='[[1os2]], [[Resolution|resolution]] 2.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | or the | + | <table><tr><td colspan='2'>[[1os2]] is a 6 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=1OS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OS2 FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1os2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1os2 OCA], [https://pdbe.org/1os2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1os2 RCSB], [https://www.ebi.ac.uk/pdbsum/1os2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1os2 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [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/os/1os2_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1os2 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Bertini I]] | |
| - | [[Category: Bertini | + | [[Category: Calderone V]] |
| - | [[Category: Calderone | + | [[Category: Fragai M]] |
| - | [[Category: Fragai | + | [[Category: Luchinat C]] |
| - | [[Category: Luchinat | + | [[Category: Mangani S]] |
| - | [[Category: Mangani | + | [[Category: Terni B]] |
| - | [[Category: Terni | + | |
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Current revision
Ternary enzyme-product-inhibitor complexes of human MMP12
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Categories: Homo sapiens | Large Structures | Bertini I | Calderone V | Fragai M | Luchinat C | Mangani S | Terni B

