› 1bue

X-ray diffraction
1.64Å 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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imipenem-hydrolyzing beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 29.14 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli
UniProt:
  • Canonical: P52663 (Residues: 28-292; Coverage: 100%)
Gene name: nmcA
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P21212
Unit cell:
a: 78.69Å b: 52.9Å c: 67.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.214
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Carbapenemases: the versatile beta-lactamases.
Queenan et al. (2007)
7 more

13 mentions without citation

Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.
Jeon et al. (2015)
12 more