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
PubMed ID
PDB structures
Hydrolytic profile
ASHV-1R164H 2135729810.1128/AAC.01360-10view
ASHV-1R164S 2135729810.1128/AAC.01360-10view
ASHV-1D104E 2129415710.1002/PROT.22961view
ASHV-1D104K 1680934010.1074/JBC.M603878200view
ASHV-1E166A 14744126view
ASHV-1E166A 1605592310.1074/JBC.M505333200view
ASHV-1E166A 2445494410.1371/JOURNAL.PONE.0085892view
ASHV-1E166A M69V 1700229010.1021/BI060990M
ASHV-1K234R 2325255310.1021/JM301490Dview
ASHV-1K234R 2445494410.1371/JOURNAL.PONE.0085892view
ASHV-1M69V 2243827410.1002/CMDC.201200006view
ASHV-1S130G 1551856110.1021/BI0487903view
ASHV-1S130G 2243827410.1002/CMDC.201200006view
ASHV-1S130G 2569163910.1128/AAC.04405-14view
ASHV-1S70C 2297428110.1021/JA3073676view

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: November 16, 2022.

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).