PDBe 1lbu

X-ray diffraction
1.8Å resolution

HYDROLASE METALLO (ZN) DD-PEPTIDASE

Released:
Source organism: Streptomyces albus G
Primary publication:
Streptomyces Albus G D-Ala-A-Ala Carboxypeptidase
Handbook of Metalloproteins 3 164- (2004)

Function and Biology Details

Reaction catalysed:
Cleavage of the bond: (Ac)(2)-L-lysyl-D-alanyl-|-D-alanine.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Zinc D-Ala-D-Ala carboxypeptidase Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 22.18 KDa
Source organism: Streptomyces albus G
UniProt:
  • Canonical: P00733 (Residues: 43-255; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 51.08Å b: 49.7Å c: 38.65Å
α: 90° β: 100.6° γ: 90°
R-values:
R R work R free
0.164 0.164 not available