+Search query
-Structure paper
Title | Antagonism between substitutions in beta-lactamase explains a path not taken in the evolution of bacterial drug resistance. |
---|---|
Journal, issue, pages | J. Biol. Chem., Vol. 295, Page 7376-7390, Year 2020 |
Publish date | Dec 4, 2019 (structure data deposition date) |
![]() | Brown, C.A. / Hu, L. / Sun, Z. / Patel, M.P. / Singh, S. / Porter, J.R. / Sankaran, B. / Prasad, B.V.V. / Bowman, G.R. / Palzkill, T. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.34 - 2.3 Å |
Structure data | ![]() PDB-6v5e: ![]() PDB-6v6g: ![]() PDB-6v6p: ![]() PDB-6v7t: ![]() PDB-6v83: ![]() PDB-6v8v: |
Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-PEG: ![]() ChemComp-NA: ![]() ChemComp-SO4: ![]() ChemComp-CAZ: |
Source |
|
![]() | HYDROLASE / drug resistance / protein evolution / conformational change / enzyme kinetics / enzyme catalysis / protein stability / protein-drug interaction / protein structure |