X-ray diffraction
1.6Å resolution

CTX-M-15 in complex with Avibactam

Source organism: Klebsiella pneumoniae
Primary publication:
Molecular Mechanism of Avibactam-Mediated ��-Lactamase Inhibition.
ACS Infect Dis 1 175-84 (2015)
PMID: 27622530

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 28.14 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
  • Canonical: G3G192 (Residues: 49-311; Coverage: 85%)
Gene name: blaCTX-M-15
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P21
Unit cell:
a: 62.01Å b: 60.65Å c: 71.5Å
α: 90° β: 104° γ: 90°
R R work R free
0.174 0.173 0.198
Expression system: Escherichia coli