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 Cited by 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: 26451738DOI: 10.1021/acs.biochem.5b01058 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (1.606 Å) X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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