› 5wad

X-ray diffraction
2.09Å resolution

ADC-7 in complex with boronic acid transition state inhibitor CR161

Released:
DOI: 10.2210/pdb5wad/pdb
PDB entry 5wad coloured by chain, front view.
PDB entry 5wad coloured by chain, side view.
PDB entry 5wad coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C β-Lactamase.
Bouza AA, Swanson HC, Smolen KA, VanDine AL, Taracila MA, Romagnoli C, Caselli E, Prati F, Bonomo RA, Powers RA, Wallar BJ
ACS Infect Dis 4 325-336 (2018)
PMID: 29144724

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 361 amino acids
Theoretical weight: 40.81 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6DRA1 (Residues: 24-383; Coverage: 100%)
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand QQZ 4 x QQZ
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 89.268Å b: 81.47Å c: 105.908Å
α: 90° β: 112.5° γ: 90°
R-values:
R R work R free
0.218 0.214 0.286
Expression system: Escherichia coli

Quick links

Citations

5 review citations

β-lactam/β-lactamase inhibitor combinations: an update.
Tehrani et al. (2018)
4 more

1 mention without citation

Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C β-Lactamase.
Bouza et al. (2018)