1ufa
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ufa' size='340' side='right'caption='[[1ufa]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1ufa' size='340' side='right'caption='[[1ufa]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ufa]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ufa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UFA FirstGlance]. <br> |
</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> | </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> | ||
| - | <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=1ufa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufa OCA], [https://pdbe.org/1ufa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ufa RCSB], [https://www.ebi.ac.uk/pdbsum/1ufa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ufa ProSAT], [https://www.topsan.org/Proteins/RSGI/1ufa TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/BE_THET8 BE_THET8]] Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin).<ref>PMID:21097495</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 06:09, 6 October 2021
Crystal structure of TT1467 from Thermus thermophilus HB8
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