Ambler class |
Protein name |
Mutations |
PubMed ID |
DOI |
PDB structures |
Hydrolytic profile |
---|---|---|---|---|---|---|
A | PC1-1 | A238S I239DEL | 8869640 | 10.1093/PROTEIN/8.12.1275 | ||
A | PC1-1 | N170D E166Q | 10436083 | 10.1093/PROTEIN/12.7.573 | ||
A | PC1-1 | N170Q | 8987980 | 10.1021/BI962242A | view | |
A | PC1-1 | N170M | 8987980 | 10.1021/BI962242A | view | |
A | PC1-1 | D179N | 1892849 | 10.1021/BI00103A017 | view | |
A | PC1-1 | E166D N170Q | 11327855 | 10.1021/BI002277H | ||
A | PC1-1 | K73H | 8823158 | 10.1021/BI961153V | view | |
A | PC1-1 | S70A | 8823158 | 10.1021/BI961153V | view |
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 20, 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 was 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