6un3

X-ray diffraction
1.9Å resolution

Crystal structure of Pseudomonas aeruginosa PBP3 in complex with ticarcillin

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.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan D,D-transpeptidase FtsI Chain: A
Molecule details ›
Chain: A
Length: 533 amino acids
Theoretical weight: 57.64 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: G3XD46 (Residues: 50-579; Coverage: 92%)
Gene names: PA4418, ftsI, pbpB
Sequence domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 68.79Å b: 83.26Å c: 89.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.267
Expression system: Escherichia coli