X-ray diffraction
2.2Å resolution

AmpC beta-lactamase in complex with 4-Amino-3-hydroxybenzoic acid

Source organism: Escherichia coli K-12
Primary publication:
Deconstructing fragment-based inhibitor discovery.
Nat. Chem. Biol. 2 720-3 (2006)
PMID: 17072304

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)
Entry contents:
1 distinct polypeptide molecule
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.59 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • 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: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 117.239Å b: 77.34Å c: 99.01Å
α: 90° β: 118.44° γ: 90°
R R work R free
0.197 0.197 0.246
Expression system: Escherichia coli