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2XR0

Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase

Summary for 2XR0
Entry DOI10.2210/pdb2xr0/pdb
Related1BZA 1IYO 1IYP 1IYQ 1IYS 1WE4 2WYX 2XQZ
DescriptorTOHO-1 BETA-LACTAMASE, SULFATE ION (3 entities in total)
Functional Keywordshydrolase, extended-spectrum beta-lactamases, esbls, ctx-m-type esbls
Biological sourceESCHERICHIA COLI
Total number of polymer chains1
Total formula weight28278.80
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 citationTomanicek, 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: 21168411
DOI: 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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