4gql

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==Crystal structure of the catalytic domain of Human MMP12 in complex with selective phosphinic inhibitor RXP470.1==
==Crystal structure of the catalytic domain of Human MMP12 in complex with selective phosphinic inhibitor RXP470.1==
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<StructureSection load='4gql' size='340' side='right' caption='[[4gql]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
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<StructureSection load='4gql' size='340' side='right'caption='[[4gql]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gql]] 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=4GQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GQL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gql]] 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=4GQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GQL 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=R47:N-[(2S)-3-[(S)-(4-BROMOPHENYL)(HYDROXY)PHOSPHORYL]-2-{[3-(3-CHLOROBIPHENYL-4-YL)-1,2-OXAZOL-5-YL]METHYL}PROPANOYL]-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMINE'>R47</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=R47:N-[(2S)-3-[(S)-(4-BROMOPHENYL)(HYDROXY)PHOSPHORYL]-2-{[3-(3-CHLOROBIPHENYL-4-YL)-1,2-OXAZOL-5-YL]METHYL}PROPANOYL]-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMINE'>R47</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]], [[3ts4|3ts4]], [[3tsk|3tsk]], [[4efs|4efs]], [[3lil|3lil]], [[3lir|3lir]], [[3ljg|3ljg]], [[4gr0|4gr0]], [[4gr3|4gr3]], [[4gr8|4gr8]]</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=4gql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gql OCA], [https://pdbe.org/4gql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gql RCSB], [https://www.ebi.ac.uk/pdbsum/4gql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gql 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=4gql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gql OCA], [http://pdbe.org/4gql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gql RCSB], [http://www.ebi.ac.uk/pdbsum/4gql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gql 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: Cassar-Lajeunesse, E]]
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[[Category: Cassar-Lajeunesse E]]
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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: Metzincin]]
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[[Category: Potent selective phosphinic inhibitor]]
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[[Category: Zinc protease]]
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Revision as of 07:10, 26 October 2022

Crystal structure of the catalytic domain of Human MMP12 in complex with selective phosphinic inhibitor RXP470.1

PDB ID 4gql

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