1mmp: Difference between revisions

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


{{STRUCTURE_1mmp|  PDB=1mmp  |  SCENE=  }}
==MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR==
 
<StructureSection load='1mmp' size='340' side='right'caption='[[1mmp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
===MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1mmp]] is a 2 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=1MMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMP FirstGlance]. <br>
{{ABSTRACT_PUBMED_7756291}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#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=RSS:5-METHYL-3-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YLCARBAMOYL)-HEXANOIC+ACID'>RSS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmp OCA], [https://pdbe.org/1mmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmp RCSB], [https://www.ebi.ac.uk/pdbsum/1mmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmp ProSAT]</span></td></tr>
[[1mmp]] is a 2 chain structure of [[Matrix metalloproteinase]] 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=1MMP OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/MMP7_HUMAN MMP7_HUMAN] Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.<ref>PMID:2550050</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mmp_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=1mmp ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:007756291</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Matrilysin]]
[[Category: Large Structures]]
[[Category: Browner, M F.]]
[[Category: Browner MF]]
[[Category: Castelhano, A L.]]
[[Category: Castelhano AL]]
[[Category: Smith, W W.]]
[[Category: Smith WW]]
[[Category: Metalloprotease]]

Latest revision as of 10:45, 14 February 2024

MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITORMATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR

Structural highlights

1mmp is a 2 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 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MMP7_HUMAN Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Quantin B, Murphy G, Breathnach R. Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry. 1989 Jun 27;28(13):5327-34. PMID:2550050

1mmp, resolution 2.30Å

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OCA
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