1wvh: Difference between revisions

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New page: left|200px<br /><applet load="1wvh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvh, resolution 1.5Å" /> '''Crystal structure of ...
 
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[[Image:1wvh.gif|left|200px]]<br /><applet load="1wvh" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of tensin1 PTB domain'''<br />


==About this Structure==
==Crystal structure of tensin1 PTB domain==
1WVH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WVH OCA].  
<StructureSection load='1wvh' size='340' side='right'caption='[[1wvh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=1wvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvh OCA], [https://pdbe.org/1wvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wvh RCSB], [https://www.ebi.ac.uk/pdbsum/1wvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TENS1_CHICK TENS1_CHICK] May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.[UniProtKB:Q9HBL0]
== 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/wv/1wvh_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=1wvh ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Liddington, R.C.]]
[[Category: Liddington RC]]
[[Category: McCleverty, C.J.]]
[[Category: McCleverty CJ]]
[[Category: beta sandwich]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:42:09 2007''

Latest revision as of 16:34, 13 March 2024

Crystal structure of tensin1 PTB domainCrystal structure of tensin1 PTB domain

Structural highlights

1wvh is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TENS1_CHICK May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.[UniProtKB:Q9HBL0]

Evolutionary Conservation

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

1wvh, resolution 1.50Å

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