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3ts4

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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=3ts4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ts4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ts4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ts4 PDBsum]</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=3ts4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ts4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ts4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ts4 PDBsum]</span></td></tr>
</table>
</table>
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== 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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 22:44, 25 December 2014

Human MMP12 in complex with L-glutamate motif inhibitor

3ts4, resolution 1.59Å

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