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-Structure paper
| Title | Structural/mechanistic insights into the efficacy of nonclassical beta-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates. |
|---|---|
| Journal, issue, pages | Mol. Microbiol., Vol. 106, Page 492-504, Year 2017 |
| Publish date | Mar 9, 2017 (structure data deposition date) |
Authors | Calvopina, K. / Hinchliffe, P. / Brem, J. / Heesom, K.J. / Johnson, S. / Cain, R. / Lohans, C.T. / Fishwick, C.W.G. / Schofield, C.J. / Spencer, J. / Avison, M.B. |
External links | Mol. Microbiol. / PubMed:28876489 |
| Methods | X-ray diffraction |
| Resolution | 1.19 - 2.09 Å |
| Structure data | ![]() PDB-5ne1: ![]() PDB-5ne2: ![]() PDB-5ne3: |
| Chemicals | ![]() ChemComp-PGE: ![]() ChemComp-OK3: ![]() ChemComp-HOH: ![]() ChemComp-DGL: ![]() ChemComp-NXL: |
| Source |
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Keywords | HYDROLASE / beta-lactamase / carbapenemase / cyclic boronate / inhibitor / Hydrolase/Inhibitor / avibactam / Hydrolase-inhibitor complex |
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stenotrophomonas maltophilia (bacteria)
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