› 1lbu

X-ray diffraction
1.8Å resolution

HYDROLASE METALLO (ZN) DD-PEPTIDASE

Released:
DOI: 10.2210/pdb1lbu/pdb
PDB entry 1lbu coloured by chain, front view.
PDB entry 1lbu coloured by chain, side view.
PDB entry 1lbu coloured by chain, top view.
Source organism: Streptomyces albus G
Primary publication:
Streptomyces Albus G D-Ala-A-Ala Carboxypeptidase
Charlier P, Wery J-P, Dideberg O, Frere J-M
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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133052 (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:
Ligand ZN 1 x ZN
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

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Citations

16 mentions without citation

A graph-theory algorithm for rapid protein side-chain prediction.
Canutescu et al. (2003)
15 more