1os9: Difference between revisions

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[[Image:1os9.png|left|200px]]


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==Binary enzyme-product complexes of human MMP12==
The line below this paragraph, containing "STRUCTURE_1os9", creates the "Structure Box" on the page.
<StructureSection load='1os9' size='340' side='right'caption='[[1os9]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1os9]] is a 6 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=1OS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OS9 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_1os9|  PDB=1os9  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1os9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1os9 OCA], [https://pdbe.org/1os9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1os9 RCSB], [https://www.ebi.ac.uk/pdbsum/1os9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1os9 ProSAT]</span></td></tr>
 
</table>
===Binary enzyme-product complexes of human MMP12===
== 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.
 
== Evolutionary Conservation ==
==About this Structure==
[[Image:Consurf_key_small.gif|200px|right]]
[[1os9]] is a 6 chain structure of [[Elastase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OS9 OCA].  
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/1os9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1os9 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Elastase]]
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:12813751</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Large Structures]]
[[Category: Bertini, I.]]
[[Category: Bertini I]]
[[Category: Calderone, V.]]
[[Category: Calderone V]]
[[Category: Fragai, M.]]
[[Category: Fragai M]]
[[Category: Luchinat, C.]]
[[Category: Luchinat C]]
[[Category: Mangani, S.]]
[[Category: Mangani S]]
[[Category: Terni, B.]]
[[Category: Terni B]]
[[Category: Elastase]]
[[Category: Hydrolase]]
[[Category: Hydroxamic acid]]
[[Category: Matrix metalloproteinase]]
[[Category: Metallo elastase]]
[[Category: Mmp12]]

Latest revision as of 12:31, 16 August 2023

Binary enzyme-product complexes of human MMP12Binary enzyme-product complexes of human MMP12

Structural highlights

1os9 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1os9, resolution 1.85Å

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