1clc
From Proteopedia
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<StructureSection load='1clc' size='340' side='right'caption='[[1clc]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1clc' size='340' side='right'caption='[[1clc]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1clc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLC OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[1clc]] 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=1CLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CLC FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1clc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clc OCA], [https://pdbe.org/1clc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1clc RCSB], [https://www.ebi.ac.uk/pdbsum/1clc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1clc ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/GUND_ACETH GUND_ACETH] 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]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Glucanase|Glucanase]] | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Acetivibrio thermocellus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Alzari | + | [[Category: Alzari PM]] |
| - | [[Category: Lascombe | + | [[Category: Lascombe MB]] |
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Current revision
THREE-DIMENSIONAL STRUCTURE OF ENDOGLUCANASE D AT 1.9 ANGSTROMS RESOLUTION
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