2vi0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:20, 13 December 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='2vi0' size='340' side='right'caption='[[2vi0]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
<StructureSection load='2vi0' size='340' side='right'caption='[[2vi0]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2vi0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VI0 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2vi0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VI0 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v0a|1v0a]], [[2bv9|2bv9]], [[2bvd|2bvd]], [[2cit|2cit]], [[2v3g|2v3g]], [[2cip|2cip]], [[2v80|2v80]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celH, Cthe_1472 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" (Viljoen et al. 1926) Yutin and Galperin 2013])</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=2vi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi0 OCA], [https://pdbe.org/2vi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vi0 RCSB], [https://www.ebi.ac.uk/pdbsum/2vi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vi0 ProSAT]</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=2vi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi0 OCA], [https://pdbe.org/2vi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vi0 RCSB], [https://www.ebi.ac.uk/pdbsum/2vi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vi0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/GUNH_CLOTH GUNH_CLOTH]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
+
[https://www.uniprot.org/uniprot/GUNH_ACET2 GUNH_ACET2] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 38: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Cellulase]]
+
[[Category: Acetivibrio thermocellus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Davies, G J]]
+
[[Category: Davies GJ]]
-
[[Category: Ducros, V M]]
+
[[Category: Ducros VM]]
-
[[Category: Money, V A]]
+
[[Category: Money VA]]
-
[[Category: Carbohydrate metabolism]]
+
-
[[Category: Cellulose degradation]]
+
-
[[Category: Enzyme glycoside hydrolase lichenase beta glucanase gh26 g]]
+
-
[[Category: Glycosidase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Polysaccharide degradation]]
+

Current revision

Lichenase CtLic26 in complex with a thio-oligosaccharide

PDB ID 2vi0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools