Beta-Lactamase DataBase
Beta-Lactamase DataBase - Structure and Function Home Enzymes Structures Mutants Kinetics BLAST
Beta-Lactamase DataBase

Synthetic Mutants (work in progress)

Ambler class
Protein name
Mutations
PubMed ID
DOI
PDB structures
Hydrolytic profile
AToho-1R274N R276N 2116841110.1016/J.FEBSLET.2010.12.017
AToho-1R274N R276N 1934278510.1107/S1744309109008240
AToho-1R274N R276N 2325559410.1074/JBC.M112.436238
AToho-1R274N R276N 10.1107/S1600576714010772
AToho-1E166A 992578610.1006/JMBI.1998.2432
AToho-1E166A 1222110210.1074/JBC.M207884200
AToho-1E166A R274N R276N 2003625910.1016/J.JMB.2009.12.036
AToho-1G238C A26M 1559582910.1021/BI048488U

Statistics (number of mutants): Overall (167); class A (91); subclass B1 (35); subclass B2 (3); subclass B3 (6); class C (19); class D (13).

Last updated: January 08, 2024.

If you use BLDB please cite: Naas, T.; Oueslati, S.; Bonnin, R. A.; Dabos, M. L.; Zavala, A.; Dortet, L.; Retailleau, P.; Iorga, B. I., Beta-Lactamase DataBase (BLDB) – Structure and Function. J. Enzyme Inhib. Med. Chem. 2017, 32, 917-919.

The development of the BLDB database is funded in part by the JPIAMR transnational project DesInMBL, the Région Ile-de-France (DIM Malinf) and the Laboratory of Excellence in Research on Medication and Innovative Therapeutics (LERMIT).

Contact: contact@bldb.eu

Live statistics (since December 3rd, 2023)