X-ray diffraction
2.1Å resolution

Crystal structure of PBP4a from Bacillus subtilis


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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
D-alanyl-D-alanine carboxypeptidase DacC Chain: A
Molecule details ›
Chain: A
Length: 462 amino acids
Theoretical weight: 49.76 KDa
Source organism: Bacillus subtilis
  • Canonical: P39844 (Residues: 30-491; Coverage: 100%)
Gene names: BSU18350, dacC, pbp
Sequence domains: D-Ala-D-Ala carboxypeptidase 3 (S13) family
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3212
Unit cell:
a: 67.411Å b: 67.411Å c: 228.464Å
α: 90° β: 90° γ: 120°
R R work R free
0.224 0.224 0.268