2k2g

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==Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor==
==Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor==
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<StructureSection load='2k2g' size='340' side='right'caption='[[2k2g]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
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<StructureSection load='2k2g' size='340' side='right'caption='[[2k2g]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2k2g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2G FirstGlance]. <br>
<table><tr><td colspan='2'>[[2k2g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSV:N-(DIBENZO[B,D]THIOPHEN-3-YLSULFONYL)-L-VALINE'>DSV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSV:N-(DIBENZO[B,D]THIOPHEN-3-YLSULFONYL)-L-VALINE'>DSV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2g OCA], [https://pdbe.org/2k2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2g RCSB], [https://www.ebi.ac.uk/pdbsum/2k2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2g ProSAT]</span></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=2k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2g OCA], [https://pdbe.org/2k2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2g RCSB], [https://www.ebi.ac.uk/pdbsum/2k2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Macrophage elastase]]
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[[Category: Dwyer B]]
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[[Category: Dwyer, B]]
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[[Category: Li J]]
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[[Category: Li, J]]
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[[Category: Li W]]
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[[Category: Li, W]]
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[[Category: Malakian K]]
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[[Category: Malakian, K]]
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[[Category: Markus MA]]
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[[Category: Markus, M A]]
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[[Category: Tsao DHH]]
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[[Category: Tsao, D H.H]]
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[[Category: Wilhelm J]]
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[[Category: Wilhelm, J]]
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[[Category: Wolfrom S]]
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[[Category: Wolfrom, S]]
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[[Category: Calcium]]
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[[Category: Catalytic domain]]
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[[Category: Extracellular matrix]]
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[[Category: Glycoprotein]]
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[[Category: Human gene]]
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[[Category: Hydrolase]]
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[[Category: Matrix metalloproteinase]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Polymorphism]]
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[[Category: Protease]]
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[[Category: Protein-ligand structure]]
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[[Category: Secreted]]
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[[Category: Zinc]]
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[[Category: Zymogen]]
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Current revision

Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor

PDB ID 2k2g

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