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2wxc
From Proteopedia
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| - | == | + | |
| - | <StructureSection load='2wxc' size='340' side='right' caption='[[2wxc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | ==The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family.== |
| + | <StructureSection load='2wxc' size='340' side='right'caption='[[2wxc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2wxc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wav 2wav]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WXC OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[2wxc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wav 2wav]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WXC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WXC FirstGlance]. <br> |
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wxc OCA], [http://pdbe.org/2wxc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wxc RCSB], [http://www.ebi.ac.uk/pdbsum/2wxc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wxc ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wx/2wxc_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wx/2wxc_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Dihydrolipoyllysine-residue succinyltransferase]] | [[Category: Dihydrolipoyllysine-residue succinyltransferase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Allen, M D]] | [[Category: Allen, M D]] | ||
[[Category: Ferguson, N]] | [[Category: Ferguson, N]] | ||
Current revision
The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family.
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