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
ACTX-M-91YLJ0.982005-04-19Q9L5C8 1581137310.1016/J.JMB.2005.02.010pdb SO4 SUC P 21 21 2141.388 62.236 85.746 ♦ 90.00 90.00 90.004
ACTX-M-91YLY1.252005-04-26Q9L5C7 1582618010.1021/JA042850Apdb *CB4 PO4 P 1 21 145.182 106.845 47.882 ♦ 90.00 101.90 90.004
ACTX-M-91YM11.122005-04-26Q9L5C8 1582618010.1021/JA042850Apdb *SM2 PO4 P 1 21 145.120 106.717 47.718 ♦ 90.00 101.89 90.004
ACTX-M-91YMS1.602005-04-26Q9L5C8 1582618010.1021/JA042850Apdb *NBF P 1 21 145.260 106.825 47.867 ♦ 90.00 101.74 90.004
ACTX-M-91YMX1.702005-04-26Q9L5C8 1582618010.1021/JA042850Apdb *CFX P 1 21 145.209 106.781 47.779 ♦ 90.00 101.62 90.004
ACTX-M-92P740.882007-04-24Q9L5C8 1740827310.1021/JA0712064pdb K PCA PO4 P 1 21 145.162 106.796 47.785 ♦ 90.00 102.09 90.004
ACTX-M-93G2Y1.312009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdbQ25PCA $GF4 DMS PCA P 1 21 145.154 106.877 47.703 ♦ 90.00 101.91 90.004
ACTX-M-93G2Z1.502009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdb $GZ2 DMS P 1 21 145.211 107.256 47.512 ♦ 90.00 101.68 90.004
ACTX-M-93G301.802009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdb $G30 P 32 2 141.803 41.803 230.542 ♦ 90.00 90.00 120.006
ACTX-M-93G311.702009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdb $GF1 DMS PO4 P 1 21 145.279 106.765 47.777 ♦ 90.00 101.74 90.004
ACTX-M-93G321.312009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdb $3G3 DMS PO4 P 1 21 145.110 107.098 47.477 ♦ 90.00 101.66 90.004
ACTX-M-93G341.312009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdb $1CE DMS PO4 P 1 21 145.141 106.886 47.445 ♦ 90.00 101.63 90.004
ACTX-M-93G351.412009-03-24Q9L5C8 1930539710.1038/NCHEMBIO.155pdb $F13 DMS P 1 21 145.265 107.243 47.727 ♦ 90.00 99.93 90.004
ACTX-M-93HLW1.502010-06-02Q9L5C8 2045235910.1016/J.JMB.2010.04.062pdbS70G $CE3 P 1 21 145.104 106.564 47.503 ♦ 90.00 101.92 90.004
ACTX-M-93HRE1.452010-06-16Q9L5C8 2045235910.1016/J.JMB.2010.04.062pdbS70G PO4 P 1 21 145.069 106.291 47.543 ♦ 90.00 102.17 90.004
ACTX-M-93HUO1.502010-05-26Q9L5C8 2045235910.1016/J.JMB.2010.04.062pdbS70G $PNK $PNN P 1 21 145.205 106.784 47.645 ♦ 90.00 101.69 90.004
ACTX-M-93HVF1.502010-05-26Q9L5C8 2045235910.1016/J.JMB.2010.04.062pdbS70G $PNK P 1 21 145.223 106.938 47.827 ♦ 90.00 101.76 90.004
ACTX-M-93Q071.502011-12-21Q9L5C8 2193088210.1128/AAC.00245-11pdbS70G $WPP $YPP P 1 21 145.128 106.340 47.610 ♦ 90.00 101.90 90.004
ACTX-M-93Q1F1.502011-12-21Q9L5C8 2193088210.1128/AAC.00245-11pdbS70G $YPP P 1 21 145.098 106.606 47.541 ♦ 90.00 101.92 90.004
ACTX-M-94DDS1.362012-03-28Q9L5C8 2229660110.1021/JM2014138pdb $0J7 DMS P 1 21 145.245 106.941 47.681 ♦ 90.00 100.97 90.004
ACTX-M-94DDY1.362012-03-28Q9L5C8 2229660110.1021/JM2014138pdb $DN6 DMS P 1 21 145.014 107.105 47.509 ♦ 90.00 102.11 90.004
ACTX-M-94DE01.122012-03-28Q9L5C8 2229660110.1021/JM2014138pdb $0JB DMS PCA P 1 21 145.192 106.565 47.669 ♦ 90.00 101.72 90.004
ACTX-M-94DE11.262012-03-28Q9L5C8 2229660110.1021/JM2014138pdb $0J6 DMS PCA P 1 21 145.166 106.567 47.825 ♦ 90.00 101.86 90.004
ACTX-M-94DE21.402012-03-28Q9L5C8 2229660110.1021/JM2014138pdb $DN3 DMS P 1 21 145.125 106.922 47.481 ♦ 90.00 101.47 90.004
ACTX-M-94DE31.442012-03-28Q9L5C8 2229660110.1021/JM2014138pdb $DN8 DMS P 1 21 145.174 107.188 47.487 ♦ 90.00 100.38 90.004
ACTX-M-94LEN1.502014-06-18Q9L5C8 2488210510.1021/JM5006572pdb *2GK P 1 21 145.116 106.595 47.680 ♦ 90.00 102.03 90.004
ACTX-M-95KMT1.702017-08-02Q9L5C8 10.1039/C7SC02676EpdbL49A K PO4 P 3241.788 41.788 232.401 ♦ 90.00 90.00 120.006
ACTX-M-95KMU1.802017-08-02Q9L5C8 10.1039/C7SC02676EpdbT165W CL PEG PO4 P 1 21 142.743 42.212 68.035 ♦ 90.00 104.52 90.002
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 (1429); class A (543); subclass B1 (348); subclass B2 (15); subclass B3 (82); class C (221); class D (220).

Last updated: November 06, 2021.

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).

Contact: contact@bldb.eu