5DPN

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

Summary for 5DPN

• Entry DOI: 10.2210/pdb5dpn/pdb
• Descriptor: Xylanase, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-[alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: carbohydrate binding module hydrogen bond h/d exchanged, sugar binding protein
• Biological source: Rhodothermus marinus
• Total number of polymer chains: 1
• Total formula weight: 19042.74

Authors

Ohlin, M. (deposition date: 2015-09-13, release date: 2015-10-28, Last modification date: 2024-05-01)

Primary citation

Fisher, S.Z.,von Schantz, L.,Hakansson, M.,Logan, D.T.,Ohlin, M.
Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.
Biochemistry, 54:6435-6438, 2015

PubMed Abstract: 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.

PubMed: 26451738
DOI: 10.1021/acs.biochem.5b01058

Experimental method

NEUTRON DIFFRACTION (1.606 Å)
X-RAY DIFFRACTION (1.6 Å)