› 4s2i

X-ray diffraction
1.6Å resolution

CTX-M-15 in complex with Avibactam

Released:
DOI: 10.2210/pdb4s2i/pdb
PDB entry 4s2i coloured by chain, front view.
PDB entry 4s2i coloured by chain, side view.
PDB entry 4s2i coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Molecular Mechanism of Avibactam-Mediated β-Lactamase Inhibition.
King DT, King AM, Lal SM, Wright GD, Strynadka NC
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124333 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: G3G192 (Residues: 49-311; Coverage: 85%)
Gene name: blaCTX-M-15
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand NXL 2 x NXL
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-values:
R R work R free
0.174 0.173 0.198
Expression system: Escherichia coli

Quick links

Citations

6 review citations

New β-Lactamase Inhibitors in the Clinic.
Papp-Wallace et al. (2016)
5 more

8 mentions without citation

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