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3dpe
From Proteopedia
(Difference between revisions)
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==Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor== | ==Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor== | ||
| - | <StructureSection load='3dpe' size='340' side='right' caption='[[3dpe]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3dpe' size='340' side='right'caption='[[3dpe]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dpe]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3dpe]] 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=3DPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DPE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AXB:N-{[2-(2-AMINO-3,4-DIOXOCYCLOBUT-1-EN-1-YL)-1,2,3,4-TETRAHYDROISOQUINOLIN-7-YL]METHYL}-4-OXO-3,5,6,8-TETRAHYDRO-4H-THIOPYRANO[4,3 4,5]THIENO[2,3-D]PYRIMIDINE-2-CARBOXAMIDE+7,7-DIOXIDE'>AXB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=AXB:N-{[2-(2-AMINO-3,4-DIOXOCYCLOBUT-1-EN-1-YL)-1,2,3,4-TETRAHYDROISOQUINOLIN-7-YL]METHYL}-4-OXO-3,5,6,8-TETRAHYDRO-4H-THIOPYRANO[4,3 4,5]THIENO[2,3-D]PYRIMIDINE-2-CARBOXAMIDE+7,7-DIOXIDE'>AXB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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">[[1xuc|1xuc]], [[1xud|1xud]], [[1xur|1xur]], [[3dng|3dng]], [[3dpf|3dpf]], [[2ow9|2ow9]], [[2ozr|2ozr]], [[1utt|1utt]], [[1utz|1utz]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xuc|1xuc]], [[1xud|1xud]], [[1xur|1xur]], [[3dng|3dng]], [[3dpf|3dpf]], [[2ow9|2ow9]], [[2ozr|2ozr]], [[1utt|1utt]], [[1utz|1utz]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP8, CLG1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP8, CLG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dpe OCA], [https://pdbe.org/3dpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dpe RCSB], [https://www.ebi.ac.uk/pdbsum/3dpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dpe ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MMP8_HUMAN MMP8_HUMAN]] Can degrade fibrillar type I, II, and III collagens. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 3dpe" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3dpe" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[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: Neutrophil collagenase]] | [[Category: Neutrophil collagenase]] | ||
[[Category: Mazza, F]] | [[Category: Mazza, F]] | ||
Revision as of 08:04, 9 February 2022
Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor
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Categories: Human | Large Structures | Neutrophil collagenase | Mazza, F | Montanari, R | Pochetti, G | Calcium | Collagen degradation | Extracellular matrix | Glycoprotein | Hydrolase | Metal-binding | Metalloprotease | Non-zinc chelating inhibitor | Polymorphism | Protease | Secreted | Selective inhibition | Zinc | Zymogen
