PDBe 1fy2

X-ray diffraction
1.2Å resolution

Aspartyl Dipeptidase

Released:

Function and Biology Details

Reaction catalysed:
Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase E Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 24.79 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P36936 (Residues: 1-229; Coverage: 100%)
Gene names: STM4190, pepE
Sequence domains: Peptidase family S51
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 91.986Å b: 42.69Å c: 62.496Å
α: 90° β: 106.06° γ: 90°
R-values:
R R work R free
0.218 0.218 0.23
Expression system: Escherichia coli