3e2k

X-ray diffraction
2.1Å resolution

Crystal Structure of the KPC-2 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP)

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-153026 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carbapenem-hydrolyzing beta-lactamase KPC Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 27.99 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 30-293; Coverage: 98%)
Gene names: bla, kpc, kpc1
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily
Beta-lactamase inhibitory protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 165 amino acids
Theoretical weight: 17.56 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli
UniProt:
  • Canonical: P35804 (Residues: 37-201; Coverage: 100%)
Sequence domains: Beta-lactamase inhibitor (BLIP)
Structure domains: Beta-lactamase Inhibitory Protein; Chain:B, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 41.24Å b: 76.198Å c: 241.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.234
Expression system: Escherichia coli