2w0d: Difference between revisions

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[[Image:2w0d.jpg|left|200px]]


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==Does a Fast Nuclear Magnetic Resonance Spectroscopy- and X-Ray Crystallography Hybrid Approach Provide Reliable Structural Information of Ligand-Protein Complexes? A Case Study of Metalloproteinases.==
The line below this paragraph, containing "STRUCTURE_2w0d", creates the "Structure Box" on the page.
<StructureSection load='2w0d' size='340' side='right'caption='[[2w0d]], [[Resolution|resolution]] 2.00&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'>[[2w0d]] is a 4 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=2W0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W0D 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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGS:N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE+HYDROCHLORIDE'>CGS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2w0d| PDB=2w0d |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0d OCA], [https://pdbe.org/2w0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w0d RCSB], [https://www.ebi.ac.uk/pdbsum/2w0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0d ProSAT]</span></td></tr>
</table>
== 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 ==
[[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/w0/2w0d_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=2w0d ConSurf].
<div style="clear:both"></div>


===DOES A FAST NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY- AND X-RAY CRYSTALLOGRAPHY HYBRID APPROACH PROVIDE RELIABLE STRUCTURAL INFORMATION OF LIGAND-PROTEIN COMPLEXES? A CASE STUDY OF METALLOPROTEINASES.===
==See Also==
 
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
2W0D is a 4 chains structure of sequences 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=2W0D OCA].
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Large Structures]]
[[Category: Agback, T.]]
[[Category: Agback T]]
[[Category: Bertini, I.]]
[[Category: Bertini I]]
[[Category: Derbyshire, D J.]]
[[Category: Derbyshire DJ]]
[[Category: Felli, I C.]]
[[Category: Felli IC]]
[[Category: Isaksson, J.]]
[[Category: Isaksson J]]
[[Category: Kovacs, H.]]
[[Category: Kovacs H]]
[[Category: Nystrom, S.]]
[[Category: Nystrom S]]
[[Category: Wallberg, H.]]
[[Category: Wallberg H]]
[[Category: Calcium]]
[[Category: Copd]]
[[Category: Extracellular matrix]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Hydroxamate]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Mmp-12]]
[[Category: Polymorphism]]
[[Category: Protease]]
[[Category: Secreted]]
[[Category: Zinc]]
[[Category: Zymogen]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar  4 14:31:59 2009''

Latest revision as of 10:09, 1 May 2024

Does a Fast Nuclear Magnetic Resonance Spectroscopy- and X-Ray Crystallography Hybrid Approach Provide Reliable Structural Information of Ligand-Protein Complexes? A Case Study of Metalloproteinases.Does a Fast Nuclear Magnetic Resonance Spectroscopy- and X-Ray Crystallography Hybrid Approach Provide Reliable Structural Information of Ligand-Protein Complexes? A Case Study of Metalloproteinases.

Structural highlights

2w0d is a 4 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 2Å
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

2w0d, resolution 2.00Å

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