› 3dw0

X-ray diffraction
1.6Å 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-108610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 31.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A8DS27 (Residues: 1-293; Coverage: 100%)
Gene names: BE932_00465, C3F40_28335, KKS20_p00170, KKS54_p00475, KKS75_p00135, KPCE_089, RZR61_18960, UC327_005, blaKPC-2, pec386IL_00095
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: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 56.3Å b: 91.3Å c: 73.1Å
α: 90° β: 112.6° γ: 90°
R-values:
R R work R free
0.189 0.188 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria.
Nordmann et al. (2009)
15 more

12 mentions without citation

Structural and Functional Aspects of Class A Carbapenemases.
Naas et al. (2016)
11 more