1lr2: Difference between revisions

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New page: left|200px<br /><applet load="1lr2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lr2, resolution 1.80Å" /> '''Crystal structure of...
 
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[[Image:1lr2.gif|left|200px]]<br /><applet load="1lr2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lr2, resolution 1.80&Aring;" />
'''Crystal structure of thaumatin at high hydrostatic pressure'''<br />


==About this Structure==
==Crystal structure of thaumatin at high hydrostatic pressure==
1LR2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii] with TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LR2 OCA].  
<StructureSection load='1lr2' size='340' side='right'caption='[[1lr2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
[[Category: Single protein]]
== Structural highlights ==
<table><tr><td colspan='2'>[[1lr2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LR2 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=1lr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lr2 OCA], [https://pdbe.org/1lr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lr2 RCSB], [https://www.ebi.ac.uk/pdbsum/1lr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lr2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
== 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/lr/1lr2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1lr2 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Thaumatococcus daniellii]]
[[Category: Capelle, B.]]
[[Category: Capelle B]]
[[Category: Charron, C.]]
[[Category: Charron C]]
[[Category: Giege, R.]]
[[Category: Giege R]]
[[Category: Kadri, A.]]
[[Category: Kadri A]]
[[Category: Lorber, B.]]
[[Category: Lorber B]]
[[Category: Robert, M.C.]]
[[Category: Robert MC]]
[[Category: TLA]]
[[Category: sweet protein]]
[[Category: taste-modifying protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:48:01 2007''

Latest revision as of 09:58, 30 October 2024

Crystal structure of thaumatin at high hydrostatic pressureCrystal structure of thaumatin at high hydrostatic pressure

Structural highlights

1lr2 is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.

Evolutionary Conservation

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

1lr2, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA