X-ray diffraction
2.1Å resolution

Crystal structure of DNPEP, ZnMg form


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

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aspartyl aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.04 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21
  • Canonical: Q2HJH1 (Residues: 3-471; Coverage: 100%)
Gene name: DNPEP
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: F432
Unit cell:
a: 244.269Å b: 244.269Å c: 244.269Å
α: 90° β: 90° γ: 90°
R R work R free
0.172 0.17 0.211
Expression system: Escherichia coli BL21