4ken

X-ray diffraction
1.89Å resolution

Crystal Structure of AmpC beta-lactamase N152G Mutant in Complex with Cefoxitin

Released:
Source organism: Escherichia coli K-12
Entry authors: Docter BE, Baggett VL, Powers RA, Wallar BJ

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: B
Molecule details ›
Chain: B
Length: 358 amino acids
Theoretical weight: 39.53 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00811 (Residues: 20-377; Coverage: 100%)
Gene names: JW4111, ampA, ampC, b4150
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: C2
Unit cell:
a: 111.192Å b: 81.488Å c: 47.386Å
α: 90° β: 105.3° γ: 90°
R-values:
R R work R free
0.16 0.158 0.2
Expression system: Escherichia coli