2XR0
Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
Summary for 2XR0
Entry DOI | 10.2210/pdb2xr0/pdb |
Related | 1BZA 1IYO 1IYP 1IYQ 1IYS 1WE4 2WYX 2XQZ |
Descriptor | TOHO-1 BETA-LACTAMASE, SULFATE ION (3 entities in total) |
Functional Keywords | hydrolase, extended-spectrum beta-lactamases, esbls, ctx-m-type esbls |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 1 |
Total formula weight | 28278.80 |
Authors | Tomanicek, S.J.,Wang, K.K.,Weiss, K.L.,Blakeley, M.P.,Cooper, J.,Chen, Y.,Coates, L. (deposition date: 2010-09-08, release date: 2010-12-22, Last modification date: 2023-12-20) |
Primary citation | Tomanicek, S.J.,Wang, K.K.,Weiss, K.L.,Blakeley, M.P.,Cooper, J.,Chen, Y.,Coates, L. The Active Site Protonation States of Perdeuterated Toho-1 Beta-Lactamase Determined by Neutron Diffraction Support a Role for Glu166 as the General Base in Acylation. FEBS Lett., 585:364-, 2011 Cited by PubMed: 21168411DOI: 10.1016/J.FEBSLET.2010.12.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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