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Probing the role of the conserved residue Glu166 in a class A β-lactamase using neutron and X-ray protein crystallography
The amino-acid sequence of the Toho-1 β-lactamase contains several conserved residues in the active site, including Ser70, Lys73, Ser130 and Glu166, some of which coordinate a catalytic water molecule. This catalytic water molecule is essential in the acylation and deacylation parts of the reaction...
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| Vydáno v: | Acta Crystallogr D Struct Biol |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2020
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7008513/ https://ncbi.nlm.nih.gov/pubmed/32038042 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2059798319016334 |
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