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4XUN

Structure of the CBM22-2 xylan-binding domain from Paenibacillus barcinonensis Xyn10C

Summary for 4XUN
Entry DOI10.2210/pdb4xun/pdb
DescriptorEndo-1,4-beta-xylanase C, CALCIUM ION (3 entities in total)
Functional Keywordsbinding site, carbohydrates, enzyme stability, substrate specificity, temperature, endo-1, 4-beta-xylanase, sugar binding protein, calcium, thermophilic enzymes, thermostabilizing domains
Biological sourcePaenibacillus barcinonensis
Total number of polymer chains3
Total formula weight59883.21
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 citationSainz-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: 26001782
DOI: 10.1074/jbc.M115.659300
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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