› 1kdw

X-ray diffraction
2.28Å resolution

X-ray crystal structure of AmpC beta-lactamase from E. coli in complex with the inhibitor 4-carboxyphenylboronic acid

Released:
DOI: 10.2210/pdb1kdw/pdb
PDB entry 1kdw coloured by chain, front view.
PDB entry 1kdw coloured by chain, side view.
PDB entry 1kdw coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure-based approach for binding site identification on AmpC beta-lactamase.
Powers RA, Shoichet BK
J Med Chem 45 3222-34 (2002)
PMID: 12109906

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 domain:

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: 358 amino acids
Theoretical weight: 39.59 KDa
Source organism: Escherichia coli
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:
Ligand PO4 1 x PO4
Ligand 4CB 2 x 4CB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 118.55Å b: 77.38Å c: 97.33Å
α: 90° β: 115.3° γ: 90°
R-values:
R R work R free
0.186 0.186 0.234
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
8 more

4 mentions without citation

Structural study of phenyl boronic acid derivatives as AmpC beta-lactamase inhibitors.
Tondi et al. (2010)
3 more