5dpn

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q7WTN6_RHOMR Q7WTN6_RHOMR]
[https://www.uniprot.org/uniprot/Q7WTN6_RHOMR Q7WTN6_RHOMR]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Carbohydrate-binding modules (CBMs) are key components of many carbohydrate-modifying enzymes. CBMs affect the activity of these enzymes by modulating bonding and catalysis. To further characterize and study CBM-ligand binding interactions, neutron crystallographic studies of an engineered family 4-type CBM in complex with a branched xyloglucan ligand were conducted. The first neutron crystal structure of a CBM-ligand complex reported here shows numerous atomic details of hydrogen bonding and water-mediated interactions and reveals the charged state of key binding cleft amino acid side chains.
 
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Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.,Fisher SZ, von Schantz L, Hakansson M, Logan DT, Ohlin M Biochemistry. 2015 Oct 27;54(42):6435-8. doi: 10.1021/acs.biochem.5b01058. Epub, 2015 Oct 13. PMID:26451738<ref>PMID:26451738</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 5dpn" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
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</StructureSection>
</StructureSection>

Current revision

Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG.

PDB ID 5dpn

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