1nzo

X-ray diffraction
1.85Å resolution

The crystal structure of wild type penicillin-binding protein 5 from E. coli

Released:

Function and Biology Details

Reactions 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.
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl-D-alanine carboxypeptidase DacA Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 39.84 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEB2 (Residues: 30-392; Coverage: 97%)
Gene names: JW0627, b0632, dacA, pfv
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 109.35Å b: 50.28Å c: 84.53Å
α: 90° β: 120.9° γ: 90°
R-values:
R R work R free
0.21 0.208 0.245
Expression system: Escherichia coli