2lab: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2lab' size='340' side='right'caption='[[2lab]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2lab' size='340' side='right'caption='[[2lab]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lab]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2lab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"aerobacillus_polymyxa"_(prazmowski_1880)_donker_1926 "aerobacillus polymyxa" (prazmowski 1880) donker 1926]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAB FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2laa|2laa]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2laa|2laa]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lab OCA], [https://pdbe.org/2lab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lab RCSB], [https://www.ebi.ac.uk/pdbsum/2lab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lab ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/AMYB_PAEPO AMYB_PAEPO]] The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion. | ||
==See Also== | ==See Also== | ||
Revision as of 10:50, 9 February 2022
Solution Strucuture of the CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxaSolution Strucuture of the CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa
Structural highlights
Function[AMYB_PAEPO] The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion. See Also |
| ||||||||||||||||