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5d2b

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==Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470==
==Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470==
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<StructureSection load='5d2b' size='340' side='right' caption='[[5d2b]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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<StructureSection load='5d2b' size='340' side='right'caption='[[5d2b]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5d2b]] 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=5D2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5d2b]] 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=5D2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D2B 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=56O:N-[(2R)-2-{[3-(3-CHLOROBIPHENYL-4-YL)-1,2-OXAZOL-5-YL]METHYL}-4-(HYDROXYAMINO)-4-OXOBUTANOYL]-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMINE'>56O</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=56O:N-[(2R)-2-{[3-(3-CHLOROBIPHENYL-4-YL)-1,2-OXAZOL-5-YL]METHYL}-4-(HYDROXYAMINO)-4-OXOBUTANOYL]-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMINE'>56O</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=5d2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2b OCA], [https://pdbe.org/5d2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d2b RCSB], [https://www.ebi.ac.uk/pdbsum/5d2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2b ProSAT]</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=5d2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2b OCA], [http://pdbe.org/5d2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2b RCSB], [http://www.ebi.ac.uk/pdbsum/5d2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2b 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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</div>
</div>
<div class="pdbe-citations 5d2b" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5d2b" style="background-color:#fffaf0;"></div>
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==See Also==
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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: 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: Rouanet-Mehouas, C]]
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[[Category: Rouanet-Mehouas C]]
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[[Category: Stura, E A]]
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[[Category: Stura EA]]
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[[Category: Hydrolase]]
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[[Category: Hydroxamate based inhibitor]]
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[[Category: Macrophage]]
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[[Category: Matrix metallo elastase]]
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[[Category: Metzincin]]
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[[Category: Mmp12]]
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[[Category: Rxp470]]
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Current revision

Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470

PDB ID 5d2b

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