4bmf
From Proteopedia
(Difference between revisions)
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<StructureSection load='4bmf' size='340' side='right'caption='[[4bmf]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''> | <StructureSection load='4bmf' size='340' side='right'caption='[[4bmf]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4bmf]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMF OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4bmf]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BMF FirstGlance]. <br> |
- | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmf OCA], [https://pdbe.org/4bmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bmf RCSB], [https://www.ebi.ac.uk/pdbsum/4bmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmf ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/GUN1_HYPJE GUN1_HYPJE]] 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. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
- | *[[Glucanase|Glucanase]] | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> |
Revision as of 07:18, 31 August 2022
Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello- oligosaccharides
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