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-Structure paper
| Title | Analysis of Nasturtium Tmnxg1 Complexes by Crystallography and Molecular Dynamics Provides Detailed Insight Into Substrate Recognition by Family Gh16 Xyloglucan Endo-Transglycosylases and Endo-Hydrolases. |
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| Journal, issue, pages | Proteins, Vol. 75, Page 820-, Year 2009 |
| Publish date | Nov 20, 2007 (structure data deposition date) |
Authors | Mark, P. / Baumann, M.J. / Eklof, J.M. / Gullfot, F. / Michel, G. / Kallas, A.M. / Teeri, T.T. / Brumer, H. / Czjzek, M. |
External links | Proteins / PubMed:19004021 |
| Methods | X-ray diffraction |
| Resolution | 2.1 Å |
| Structure data | ![]() PDB-2vh9: |
| Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-GOL: ![]() ChemComp-BGC: ![]() ChemComp-HOH: |
| Source |
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Keywords | HYDROLASE / GLYCOSIDASE / FAMILY GH16 / TROPAEOLUM MAJUS XYLOGLUCANASE / XLLG OLIGOSACCHARIDE / LOOP MUTANT NXG1-YNIIG / SUBSTRATE COMPLEX / GLYCOSIDE HYDROLASE |
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tropaeolum majus (nasturtium)
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