3a3e

X-ray diffraction
2.4Å resolution

Crystal structure of penicillin binding protein 4 (dacB) from Haemophilus influenzae, complexed with novel beta-lactam (CMV)

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-binding protein 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 453 amino acids
Theoretical weight: 49.79 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: A8E0K8 (Residues: 28-479; Coverage: 94%)
Gene name: dacB
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 64.898Å b: 92.823Å c: 104.173Å
α: 90° β: 107.79° γ: 90°
R-values:
R R work R free
0.22 0.217 0.28
Expression system: Escherichia coli