1ulo: Difference between revisions

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 ==N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, MINIMIZED AVERAGE STRUCTURE==
-<StructureSection load='1ulo' size='340' side='right'caption='[[1ulo]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1ulo' size='340' side='right'caption='[[1ulo]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ulo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_fimi"_mcbeth_and_scales_1913 "bacterium fimi" mcbeth and scales 1913]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ulo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULO FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ulp|1ulp]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1ulo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulo OCA], [https://pdbe.org/1ulo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulo RCSB], [https://www.ebi.ac.uk/pdbsum/1ulo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GUNC_CELFA GUNC_CELFA]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
+[https://www.uniprot.org/uniprot/GUNC_CELFA GUNC_CELFA] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Bacterium fimi mcbeth and scales 1913]]
+[[Category: Cellulomonas fimi]]
-[[Category: Cellulase]]
 [[Category: Large Structures]]
-[[Category: Johnson, P E]]
+[[Category: Johnson PE]]
-[[Category: Mcintosh, L P]]
+[[Category: Mcintosh LP]]
-[[Category: Cellulose degradation]]
-[[Category: Cellulose-binding domain]]
-[[Category: Hydrolase]]