5JRM
Crystal Structure of a Xylanase at 1.56 Angstroem resolution
Summary for 5JRM
| Entry DOI | 10.2210/pdb5jrm/pdb |
| Descriptor | Endo-1,4-beta-xylanase, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | xylanase, gh11, hydrolase |
| Biological source | Fusarium oxysporum |
| Total number of polymer chains | 1 |
| Total formula weight | 21625.33 |
| Authors | Gomez, S.,Payne, A.M.,Savko, M.,Fox, G.C.,Shepard, W.E.,Fernandez, F.J.,Vega, M.C. (deposition date: 2016-05-06, release date: 2017-05-24, Last modification date: 2024-10-23) |
| Primary citation | Gomez, S.,Payne, A.M.,Savko, M.,Fox, G.C.,Shepard, W.E.,Fernandez, F.J.,Cristina Vega, M. Structural and functional characterization of a highly stable endo-beta-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst. Biotechnol Biofuels, 9:191-191, 2016 Cited by PubMed Abstract: Replacing fossil fuel with renewable sources such as lignocellulosic biomass is currently a promising alternative for obtaining biofuel and for fighting against the consequences of climate change. However, the recalcitrant structure of lignocellulosic biomass residues constitutes a major limitation for its widespread use in industry. The efficient hydrolysis of lignocellulosic materials requires the complementary action of multiple enzymes including xylanases and β-xylosidases, which are responsible for cleaving exo- and endoxylan linkages, that release oligocarbohydrates that can be further processed by other enzymes. PubMed: 27602054DOI: 10.1186/s13068-016-0605-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
Download full validation report
