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4efs

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==Human MMP12 in complex with L-glutamate motif inhibitor==
==Human MMP12 in complex with L-glutamate motif inhibitor==
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<StructureSection load='4efs' size='340' side='right' caption='[[4efs]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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<StructureSection load='4efs' size='340' side='right'caption='[[4efs]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4efs]] 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=4EFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EFS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4efs]] 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=4EFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EFS FirstGlance]. <br>
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</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=E37:N~2~-[4-(4-PHENYLTHIOPHEN-2-YL)BENZOYL]-L-ALPHA-GLUTAMINE'>E37</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=PGR:R-1,2-PROPANEDIOL'>PGR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E37:N~2~-[4-(4-PHENYLTHIOPHEN-2-YL)BENZOYL]-L-ALPHA-GLUTAMINE'>E37</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=PGR:R-1,2-PROPANEDIOL'>PGR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lik|3lik]], [[3lil|3lil]], [[3lir|3lir]], [[3ljg|3ljg]], [[3ts4|3ts4]]</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=4efs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efs OCA], [https://pdbe.org/4efs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4efs RCSB], [https://www.ebi.ac.uk/pdbsum/4efs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4efs ProSAT]</span></td></tr>
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<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>
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<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>
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<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=4efs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efs OCA], [http://pdbe.org/4efs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4efs RCSB], [http://www.ebi.ac.uk/pdbsum/4efs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4efs ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Matrix metalloproteinase|Matrix metalloproteinase]]
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*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Macrophage elastase]]
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[[Category: Large Structures]]
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[[Category: Beau, F]]
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[[Category: Beau F]]
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[[Category: Czarny, B]]
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[[Category: Czarny B]]
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[[Category: Devel, L]]
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[[Category: Devel L]]
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[[Category: Dive, V]]
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[[Category: Dive V]]
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[[Category: Stura, E A]]
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[[Category: Stura EA]]
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[[Category: Vera, L]]
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[[Category: Vera L]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: L-glutamate motif inhibitor]]
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[[Category: Metzincin]]
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[[Category: Potent inhibitor]]
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[[Category: Pseudo peptide]]
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[[Category: Zinc protease]]
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Revision as of 07:09, 28 September 2022

Human MMP12 in complex with L-glutamate motif inhibitor

PDB ID 4efs

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