3f19: Difference between revisions

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==Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor 4-fluoro-N-(2-nitroso-2-oxoethyl)benzenesulfonamide==
==Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor 4-fluoro-N-(2-nitroso-2-oxoethyl)benzenesulfonamide==
<StructureSection load='3f19' size='340' side='right' caption='[[3f19]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
<StructureSection load='3f19' size='340' side='right'caption='[[3f19]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3f19]] 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=3F19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F19 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3f19]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F19 FirstGlance]. <br>
</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=HS6:2-[(4-FLUOROPHENYL)SULFONYLAMINO]-N-OXO-ETHANAMIDE'>HS6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</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=HS6:2-[(4-FLUOROPHENYL)SULFONYLAMINO]-N-OXO-ETHANAMIDE'>HS6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f15|3f15]], [[3f16|3f16]], [[3f17|3f17]], [[3f18|3f18]], [[3f1a|3f1a]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3f15|3f15]], [[3f16|3f16]], [[3f17|3f17]], [[3f18|3f18]], [[3f1a|3f1a]]</div></td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HME, MMP12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3f19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f19 OCA], [http://pdbe.org/3f19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f19 RCSB], [http://www.ebi.ac.uk/pdbsum/3f19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f19 ProSAT]</span></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=3f19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f19 OCA], [https://pdbe.org/3f19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f19 RCSB], [https://www.ebi.ac.uk/pdbsum/3f19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f19 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[[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.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Calderone, V]]
[[Category: Calderone, V]]
[[Category: Calcium]]
[[Category: Calcium]]
Retrieved from "https://proteopedia.org/3f19"