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Title | Bacteroides thetaiotaomicron generates diverse alpha-mannosidase activities through subtle evolution of a distal substrate-binding motif. |
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Journal, issue, pages | Acta Crystallogr D Struct Biol, Vol. 74, Page 394-404, Year 2018 |
Publish date | Dec 13, 2017 (structure data deposition date) |
![]() | Thompson, A.J. / Spears, R.J. / Zhu, Y. / Suits, M.D.L. / Williams, S.J. / Gilbert, H.J. / Davies, G.J. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.8 - 2.5 Å |
Structure data | ![]() PDB-6f8z: ![]() PDB-6f90: ![]() PDB-6f91: ![]() PDB-6f92: |
Chemicals | ![]() ChemComp-CA: ![]() ChemComp-EDO: ![]() ChemComp-HOH: ![]() ChemComp-MVL: ![]() ChemComp-NA: ![]() ChemComp-CL: ![]() ChemComp-NO3: |
Source |
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![]() | HYDROLASE / glycan / carbohydrate / glycosidase / substrate specificity / glycoside hydrolase / alpha-mannosidase / GH92 / gut bacteria / microbiota / CAZy / CAZypedia |