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==Crystal structure of tryptophan synthase beta chain from Thermus thermophilus HB8== | ==Crystal structure of tryptophan synthase beta chain from Thermus thermophilus HB8== | ||
<StructureSection load='1x1q' size='340' side='right' caption='[[1x1q]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1x1q' size='340' side='right'caption='[[1x1q]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1x1q]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1x1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X1Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1x1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1q OCA], [https://pdbe.org/1x1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x1q RCSB], [https://www.ebi.ac.uk/pdbsum/1x1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x1q ProSAT], [https://www.topsan.org/Proteins/RSGI/1x1q TOPSAN]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TRPB_THET2 TRPB_THET2] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x1/1x1q_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x1/1x1q_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1x1q ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Tryptophan synthase|Tryptophan synthase]] | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Asada | [[Category: Asada Y]] | ||
[[Category: Kunishima | [[Category: Kunishima N]] | ||
Latest revision as of 10:35, 30 October 2024
Crystal structure of tryptophan synthase beta chain from Thermus thermophilus HB8Crystal structure of tryptophan synthase beta chain from Thermus thermophilus HB8
Structural highlights
FunctionTRPB_THET2 The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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