› 4n92

X-ray diffraction
1.93Å resolution

Crystal structure of beta-lactamse PenP_E166S

Released:
DOI: 10.2210/pdb4n92/pdb
PDB entry 4n92 coloured by chain, front view.
PDB entry 4n92 coloured by chain, side view.
PDB entry 4n92 coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Perturbing the general base residue Glu166 in the active site of class A β-lactamase leads to enhanced carbapenem binding and acylation.
Pan X, Wong WT, He Y, Jiang Y, Zhao Y
Biochemistry 53 5414-23 (2014)
PMID: 25020031

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 29.79 KDa
Source organism: Bacillus licheniformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P00808 (Residues: 43-307; Coverage: 94%)
Gene names: blaP, penP
Sequence domains: Beta-lactamase
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: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 43.31Å b: 46.19Å c: 66.28Å
α: 78.43° β: 75.71° γ: 69.36°
R-values:
R R work R free
0.18 0.177 0.23
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Prevalence and Fate of Carbapenemase Genes in a Wastewater Treatment Plant in Northern China.
Yang et al. (2016)
5 more