PDBe 4dyo

X-ray diffraction
2.2Å resolution

Crystal Structure of Human Aspartyl Aminopeptidase (DNPEP) in complex with Aspartic acid Hydroxamate

Released:

Function and Biology Details

Reaction catalysed:
Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo 12-mer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartyl aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 485 amino acids
Theoretical weight: 53.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ULA0 (Residues: 1-468; Coverage: 99%)
Gene names: ASPEP, DAP, DNPEP
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: F432
Unit cell:
a: 244.595Å b: 244.595Å c: 244.595Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.155 0.195
Expression system: Escherichia coli BL21(DE3)