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1clc

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1clc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1clc RCSB], [http://www.ebi.ac.uk/pdbsum/1clc PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1clc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1clc RCSB], [http://www.ebi.ac.uk/pdbsum/1clc PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GUND_CLOTM GUND_CLOTM]] 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]]

Revision as of 18:50, 25 December 2014

THREE-DIMENSIONAL STRUCTURE OF ENDOGLUCANASE D AT 1.9 ANGSTROMS RESOLUTION

1clc, resolution 1.90Å

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