4XUT
Structure of the CBM22-2 xylan-binding domain in complex with 1,3:1,4 Beta-glucotetraose B from Paenibacillus barcinonensis Xyn10C
Summary for 4XUT
Entry DOI | 10.2210/pdb4xut/pdb |
Related PRD ID | PRD_900005 |
Descriptor | Endo-1,4-beta-xylanase C, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | carbohydrates, enzyme stability, substrate specificity, endo-1, 4-beta-xylanase, xylan-binding domain, thermophilic enzymes, thermostabilizing domains, 1, 3:1, 4 beta-glucotetraose b, sugar binding protein |
Biological source | Paenibacillus barcinonensis |
Total number of polymer chains | 3 |
Total formula weight | 60225.51 |
Authors | Sainz-Polo, M.A.,Sanz-Aparicio, J. (deposition date: 2015-01-26, release date: 2015-06-03, Last modification date: 2024-01-10) |
Primary citation | Sainz-Polo, M.A.,Gonzalez, B.,Menendez, M.,Pastor, F.I.,Sanz-Aparicio, J. Exploring Multimodularity in Plant Cell Wall Deconstruction: STRUCTURAL AND FUNCTIONAL ANALYSIS OF Xyn10C CONTAINING THE CBM22-1-CBM22-2 TANDEM. J.Biol.Chem., 290:17116-17130, 2015 Cited by PubMed: 26001782DOI: 10.1074/jbc.M115.659300 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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