3ue3

X-ray diffraction
2.3Å resolution

Crystal structure of Acinetobacter baumanni PBP3

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)
PDBe Complex ID:
PDB-CPX-111063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan D,D-transpeptidase FtsI Chain: A
Molecule details ›
Chain: A
Length: 554 amino acids
Theoretical weight: 61.17 KDa
Source organism: Acinetobacter sp. ATCC 27244
Expression system: Escherichia coli
UniProt:
  • Canonical: C0VN42 (Residues: 64-609; Coverage: 90%)
Gene names: HMPREF0023_2561, ftsI
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 39.657Å b: 89.707Å c: 211.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.217 0.25
Expression system: Escherichia coli