X-ray diffraction
1.1Å resolution

penicilloyl acyl enzyme complex of the Streptomyces R61 DD-peptidase with penicillin G


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
D-alanyl-D-alanine carboxypeptidase Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 37.42 KDa
Source organism: Streptomyces sp. R61
  • Canonical: P15555 (Residues: 32-380; Coverage: 93%)
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 50.9Å b: 66.7Å c: 99.6Å
α: 90° β: 90° γ: 90°
R R work R free
0.124 0.12 0.148