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| Title | Family GH157 enzyme exhibits broad linkage tolerance and a dual endo/exo-beta-glucanase activity on beta-glucans. |
|---|---|
| Journal, issue, pages | Int. J. Biol. Macromol., Vol. 282, Page 137402-137402, Year 2024 |
| Publish date | Jul 4, 2024 (structure data deposition date) |
Authors | Caseiro, C. / McGregor, N.G.S. / Alves, V.D. / Carvalho, A.L. / Romao, M.J. / Davies, G.J. / Fontes, C.M.G.A. / Bule, P. |
External links | Int. J. Biol. Macromol. / PubMed:39528173 |
| Methods | X-ray diffraction |
| Resolution | 2.32 - 2.71 Å |
| Structure data | ![]() PDB-9fz9: ![]() PDB-9g4n: ![]() PDB-9g5g: |
| Chemicals | ![]() ChemComp-ACT: ![]() ChemComp-GOL: ![]() ChemComp-MLA: ![]() ChemComp-HOH: ![]() ChemComp-EDO: ![]() ChemComp-BGC: ![]() ChemComp-PGE: ![]() ChemComp-PG4: |
| Source |
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Keywords | HYDROLASE / GH157 / endo-1 / 3(4)-beta-glucanase / Labilibaculum antarcticum / Wild type SeMet derivative / glycoside hydrolase / endo-beta-1 / 3-glucanase / cazyme / ligand complex |
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labilibaculum antarcticum (bacteria)
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