5lab: Difference between revisions
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New page: '''Unreleased structure''' The entry 5lab is ON HOLD Authors: Ravera, E., Calderone, V., Luchinat, C. Description: Crystal structure of the catalytic domain of human MMP12 complexed wi... |
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==Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH== | |||
<StructureSection load='5lab' size='340' side='right'caption='[[5lab]], [[Resolution|resolution]] 1.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lab]] 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=5LAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LAB 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]] 1.34Å</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=NGH:N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL+HYDROXAMIC+ACID'>NGH</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=5lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lab OCA], [https://pdbe.org/5lab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lab RCSB], [https://www.ebi.ac.uk/pdbsum/5lab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lab 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. | |||
==See Also== | |||
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Calderone | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Calderone V]] | ||
[[Category: Luchinat C]] | |||
[[Category: Ravera E]] | |||
Latest revision as of 10:48, 7 February 2024
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGHCrystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH
Structural highlights
FunctionMMP12_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. See Also |
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