1sdn

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF A DEACYLATION-DEFECTIVE MUTANT OF PENICILLIN-BINDING PROTEIN 5 MODIFIED BY MERCURY

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: 39.9 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: ENRAF-NONIUS FR591
Spacegroup: P32
Unit cell:
a: 50.7Å b: 50.7Å c: 140.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.171 0.241
Expression system: Escherichia coli