4i5u

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==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==
==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==
<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
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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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [http://www.ebi.ac.uk/pdbsum/4i5u PDBsum]</span></td></tr>
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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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [http://pdbe.org/4i5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [http://www.ebi.ac.uk/pdbsum/4i5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i5u ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GUX6_HUMIN GUX6_HUMIN]] Plays a central role in the recycling of plant biomass. 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.<ref>PMID:9882628</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4i5u" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 21:23, 5 August 2016

Crystal structure of a fungal chimeric cellobiohydrolase Cel6A

4i5u, resolution 1.22Å

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