PDBe 1ei5

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI

Released:

Function and Biology Details

Reaction catalysed:
Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-Amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 520 amino acids
Theoretical weight: 57.46 KDa
Source organism: Ochrobactrum anthropi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZBA9 (Residues: 1-520; Coverage: 100%)
Gene name: dap
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P41212
Unit cell:
a: 82.86Å b: 82.86Å c: 204.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.163 0.192
Expression system: Escherichia coli