2jf4: Difference between revisions
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==Family 37 trehalase from Escherichia coli in complex with validoxylamine== | |||
<StructureSection load='2jf4' size='340' side='right'caption='[[2jf4]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
=== | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jf4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JF4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VDM:(1S,2S,3R,6S)-4-(HYDROXYMETHYL)-6-{[(1S,2S,3S,4R,5R)-2,3,4-TRIHYDROXY-5-(HYDROXYMETHYL)CYCLOHEXYL]AMINO}CYCLOHEX-4-ENE-1,2,3-TRIOL'>VDM</scene></td></tr> | |||
== | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
[[2jf4]] is a 1 chain structure with sequence from [ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha,alpha-trehalase Alpha,alpha-trehalase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.28 3.2.1.28] </span></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=2jf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jf4 OCA], [https://pdbe.org/2jf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jf4 RCSB], [https://www.ebi.ac.uk/pdbsum/2jf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jf4 ProSAT]</span></td></tr> | |||
== | </table> | ||
< | == Function == | ||
[[https://www.uniprot.org/uniprot/TREA_ECOLI TREA_ECOLI]] Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.[HAMAP-Rule:MF_01060] | |||
== 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/jf/2jf4_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=2jf4 ConSurf]. | |||
<div style="clear:both"></div> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alpha,alpha-trehalase]] | [[Category: Alpha,alpha-trehalase]] | ||
[[Category: | [[Category: Ecoli]] | ||
[[Category: Chiara, J L | [[Category: Large Structures]] | ||
[[Category: Davies, G J | [[Category: Chiara, J L]] | ||
[[Category: Garcia, A | [[Category: Davies, G J]] | ||
[[Category: Gibson, R P | [[Category: Garcia, A]] | ||
[[Category: Gloster, T M | [[Category: Gibson, R P]] | ||
[[Category: Gracia, I Storch De | [[Category: Gloster, T M]] | ||
[[Category: Roberts, S | [[Category: Gracia, I Storch De]] | ||
[[Category: Warren, R A.J | [[Category: Roberts, S]] | ||
[[Category: Warren, R A.J]] | |||
[[Category: Family 37]] | [[Category: Family 37]] | ||
[[Category: Glycosidase]] | [[Category: Glycosidase]] | ||
Latest revision as of 11:09, 19 January 2022
Family 37 trehalase from Escherichia coli in complex with validoxylamineFamily 37 trehalase from Escherichia coli in complex with validoxylamine
Structural highlights
Function[TREA_ECOLI] Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.[HAMAP-Rule:MF_01060] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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