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2wxc
From Proteopedia
(Difference between revisions)
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| - | == | + | |
| + | ==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=''> | <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 | + | <table><tr><td colspan='2'>[[2wxc]] is a 1 chain structure. 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://oca.weizmann.ac.il/oca-docs/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://oca.weizmann.ac.il/oca-docs/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]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Dihydrolipoyllysine-residue succinyltransferase]] | [[Category: Dihydrolipoyllysine-residue succinyltransferase]] | ||
[[Category: Allen, M D]] | [[Category: Allen, M D]] | ||
Revision as of 06:04, 19 April 2017
The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family.
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