› 1lfw

X-ray diffraction
1.8Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-Ala-Xaa dipeptidase Chain: A
Molecule details ›
Chain: A
Length: 470 amino acids
Theoretical weight: 52.05 KDa
Source organism: Lactobacillus delbrueckii subsp. lactis
Expression system: Escherichia coli
UniProt:
  • Canonical: P45494 (Residues: 1-470; Coverage: 100%)
Gene name: pepV
Sequence domains: Peptidase family M20/M25/M40
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand AEP 1 x AEP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 67.151Å b: 77.025Å c: 89.955Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Carnosinases, their substrates and diseases.
Bellia et al. (2014)
3 more

9 mentions without citation

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.
Georgiadis et al. (2022)
8 more