› 5ne2

X-ray diffraction
1.19Å resolution

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193129 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 278 amino acids
Theoretical weight: 29.32 KDa
Source organism: Stenotrophomonas maltophilia
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RBQ1 (Residues: 28-303; Coverage: 100%)
Gene names: L2, blaL2
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand DGL 2 x DGL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 69.678Å b: 84.72Å c: 93.712Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.152 0.164
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
4 more

2 mentions without citation

The Role of the Ω-Loop in Regulation of the Catalytic Activity of TEM-Type β-Lactamases.
Egorov et al. (2019)
1 more