Beta-Lactamase DataBase (BLDB): Structure and Function

Ambler class	Protein name	PDB code	Resolution (Å)	Release date	UniProt code	PubMed ID	DOI	PDB	Ligands	Space group	Unit cell parameters	Z value
▲ ▼	▲ ▼	▲ ▼	▲ ▼	▲ ▼						▲ ▼
A	CTX-M-151	6BN3	1.28	2018-11-21	A0A077KT80	33431411	10.1128/AAC.01757-20	pdb	EPE	C 1 2 1	95.790 41.810 56.450 ♦ 90.00 94.14 90.00	4
A	CTX-M-151	6BPF	1.32	2018-11-28	A0A077KT80	33431411	10.1128/AAC.01757-20	pdb	*NXL	C 1 2 1	95.590 41.940 56.360 ♦ 90.00 94.09 90.00	4

Legend for ligands: * Ligand covalently-bound to active site residues; ^$ Non-covalent ligand (Michaelis complex); ^# Ligand coordinated to active site metal ions.

Statistics (number of structures): Overall (1663); class A (626); subclass B1 (403); subclass B2 (16); subclass B3 (104); class C (246); class D (268).

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

Live statistics (since December 3rd, 2023)

Structures