1x1q: Difference between revisions
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==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=''> | |||
== Structural highlights == | |||
<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='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='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> | ||
[[1x1q]] is a 2 chain structure with sequence from [ | <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> | ||
</table> | |||
== 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 == | |||
[[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/x1/1x1q_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=1x1q ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Asada Y]] | |||
[[Category: | [[Category: Kunishima N]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
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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