› 1mxo

X-ray diffraction
1.83Å resolution

AmpC beta-lactamase in complex with an m.carboxyphenylglycylboronic acid bearing the cephalothin R1 side chain

Released:
DOI: 10.2210/pdb1mxo/pdb
PDB entry 1mxo coloured by chain, front view.
PDB entry 1mxo coloured by chain, side view.
PDB entry 1mxo coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Nanomolar inhibitors of AmpC beta-lactamase.
Morandi F, Caselli E, Morandi S, Focia PJ, Blázquez J, Shoichet BK, Prati F
J Am Chem Soc 125 685-95 (2003)
PMID: 12526668

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 K-12
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 SM2 2 x SM2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 117.957Å b: 77.488Å c: 96.906Å
α: 90° β: 115.78° γ: 90°
R-values:
R R work R free
0.187 0.187 0.214
Expression system: Escherichia coli K-12

Quick links

Citations

15 review citations

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

7 mentions without citation

Inhibition of the class C beta-lactamase from Acinetobacter spp.: insights into effective inhibitor design.
Drawz et al. (2010)
6 more