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; PubMed: 26001782; DOI: 10.1074/jbc.M115.659300

Experimental method

X-RAY DIFFRACTION (1.8 Å)