Beta-Lactamase DataBase
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Beta-Lactamase DataBase

Structures

Ambler
class
Protein
name
PDB
code
Resolution
(Å)
Release
date
UniProt
code
PubMed
ID
DOI
PDB
Mutations
Ligands
Space
group
Unit cell parameters
Z
value
AKPC-448TJM1.282023-12-06A0A4Y5JTU1 3800065610.1016/J.JBC.2023.105493pdb EDO SO4 P 32 2 172.180 72.180 84.981 ♦ 90.00 90.00 120.006
AKPC-448TMR1.372023-12-06A0A4Y5JTU1 3800065610.1016/J.JBC.2023.105493pdb *NXL EDO PO4 P 32 2 171.760 71.760 84.580 ♦ 90.00 90.00 120.006
AKPC-448TMT1.702023-12-06A0A4Y5JTU1 3800065610.1016/J.JBC.2023.105493pdb *4D6 EDO GOL LI NA SO4 P 32 2 172.380 72.380 85.500 ♦ 90.00 90.00 120.006
AKPC-448TN01.312023-12-06A0A4Y5JTU1 3800065610.1016/J.JBC.2023.105493pdb SO4 P 32 2 172.338 72.338 84.715 ♦ 90.00 90.00 120.006
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)