› 4gzb

X-ray diffraction
1.79Å resolution

Crystal structure of native AmpC beta-lactamase from Pseudomonas aeruginosa PAO1

Released:
DOI: 10.2210/pdb4gzb/pdb
PDB entry 4gzb coloured by chain, front view.
PDB entry 4gzb coloured by chain, side view.
PDB entry 4gzb coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-lactamases.
Lahiri SD, Mangani S, Durand-Reville T, Benvenuti M, De Luca F, Sanyal G, Docquier JD
Antimicrob Agents Chemother 57 2496-505 (2013)
PMID: 23439634

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150279 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 40.72 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: P24735 (Residues: 27-397; Coverage: 100%)
Gene names: PA4110, ampC
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 83.06Å b: 83.06Å c: 122.42Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.19 0.244
Expression system: Escherichia coli

Quick links

Citations

32 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
31 more

15 mentions without citation

Resistance to Novel β-Lactam-β-Lactamase Inhibitor Combinations: The "Price of Progress".
Papp-Wallace et al. (2020)
14 more