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-Structure paper
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) |
Authors | Thompson, A.J. / Spears, R.J. / Zhu, Y. / Suits, M.D.L. / Williams, S.J. / Gilbert, H.J. / Davies, G.J. |
External links | Acta Crystallogr D Struct Biol / PubMed:29717710 |
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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Keywords | HYDROLASE / glycan / carbohydrate / glycosidase / substrate specificity / glycoside hydrolase / alpha-mannosidase / GH92 / gut bacteria / microbiota / CAZy / CAZypedia |