› 6jn6

X-ray diffraction
1.6Å resolution

Metallo-Beta-Lactamase VIM-2 in complex with Dual MBL/SBL Inhibitor MS19

Released:
DOI: 10.2210/pdb6jn6/pdb
PDB entry 6jn6 coloured by chain, front view.
PDB entry 6jn6 coloured by chain, side view.
PDB entry 6jn6 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structure-Based Development of (1-(3'-Mercaptopropanamido)methyl)boronic Acid Derived Broad-Spectrum, Dual-Action Inhibitors of Metallo- and Serine-β-lactamases.
Wang YL, Liu S, Yu ZJ, Lei Y, Huang MY, Yan YH, Ma Q, Zheng Y, Deng H, Sun Y, Wu C, Yu Y, Chen Q, Wang Z, Wu Y, Li GB
J Med Chem 62 7160-7184 (2019)
PMID: 31269398

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 231 amino acids
Theoretical weight: 24.68 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K2N0 (Residues: 32-262; Coverage: 94%)
Gene names: PAERUG_P19_London_7_VIM_2_05_10_01672, bla vim-2, blaVIM-2, blm
Sequence domains: Metallo-beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand ZN 6 x ZN
Ligand BY0 2 x BY0
Ligand FMT 6 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: C2
Unit cell:
a: 102.51Å b: 79.236Å c: 67.806Å
α: 90° β: 130.61° γ: 90°
R-values:
R R work R free
0.157 0.156 0.187
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
4 more