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-Structure paper
| Title | Structure-function analyses reveal that a glucuronoyl esterase fromTeredinibacter turneraeinteracts with carbohydrates and aromatic compounds. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 294, Page 6635-6644, Year 2019 |
| Publish date | Oct 2, 2018 (structure data deposition date) |
Authors | Arnling Baath, J. / Mazurkewich, S. / Poulsen, J.N. / Olsson, L. / Lo Leggio, L. / Larsbrink, J. |
External links | J. Biol. Chem. / PubMed:30814248 |
| Methods | X-ray diffraction |
| Resolution | 2.14734381231 Å |
| Structure data | ![]() PDB-6hsw: |
| Chemicals | ![]() ChemComp-1PE: ![]() ChemComp-EDO: ![]() ChemComp-GOL: ![]() ChemComp-BR: ![]() ChemComp-PEG: ![]() ChemComp-HOH: |
| Source |
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Keywords | HYDROLASE / CE15 / carbohydrate esterase / glucuronoyl esterase / xylan |
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teredinibacter turnerae t7901 (bacteria)
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