› 5joc

X-ray diffraction
1.75Å resolution

Crystal structure of the S61A mutant of AmpC BER

Released:
DOI: 10.2210/pdb5joc/pdb
PDB entry 5joc coloured by chain, front view.
PDB entry 5joc coloured by chain, side view.
PDB entry 5joc coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C β-lactamases AmpC BER and CMY-10.
Na JH, Cha SS
Acta Crystallogr D Struct Biol 72 976-85 (2016)
PMID: 27487828

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
Sequence domains:

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 40.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00811 (Residues: 21-311, 312-377; Coverage: 100%)
Gene names: JW4111, ampA, ampC, b4150
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand CIT 4 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P63
Unit cell:
a: 207.208Å b: 207.208Å c: 45.635Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.177 0.2
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Class C β-Lactamases: Molecular Characteristics.
Philippon et al. (2022)
4 other articles

1 mention without citation

Structural Basis of Reduced Susceptibility to Ceftazidime-Avibactam and Cefiderocol in Enterobacter cloacae Due to AmpC R2 Loop Deletion.
Kawai et al. (2020)