7onw

X-ray diffraction
2.7Å resolution

Crystal structure of PBP3 from E. coli in complex with AIC499

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: 564 amino acids
Theoretical weight: 61.1 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AD68 (Residues: 49-588; Coverage: 92%)
Gene names: JW0082, b0084, ftsI, pbpB
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6422
Unit cell:
a: 106.904Å b: 106.904Å c: 285.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.234 0.271
Expression system: Escherichia coli BL21(DE3)