Beta-Lactamase DataBase
Beta-Lactamase DataBase - Structure and Function Home Enzymes Structures Mutants Kinetics BLAST
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
ASED-13BFC2.202007-12-18Q93PQ0 pdbG238C *IM2 C 1 2 1188.436 73.399 105.050 ♦ 90.00 122.36 90.0016
ASED-13BFD2.002007-12-18Q93PQ0 pdbG238C CAC C 1 2 1187.642 73.200 103.893 ♦ 90.00 121.89 90.0016
ASED-13BFE2.402007-12-18Q93PQ0 pdb SCN C 1 2 1188.099 73.655 105.409 ♦ 90.00 121.67 90.0016
ASED-13BFF1.902007-12-18Q93PQ0 pdbG238C $FPM *SFR SCN C 1 2 1187.116 73.244 103.504 ♦ 90.00 121.69 90.0016
ASED-13BFG2.002007-12-18Q93PQ0 pdbG238C *MER C 1 2 1188.142 73.177 105.384 ♦ 90.00 122.42 90.0016
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)