PDBe 4nol

X-ray diffraction
2.7Å resolution

Crystal structure of proenzyme asparaginyl endopeptidase (AEP)/Legumain mutant D233A at pH 7.5


Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Legumain Chains: A, B
Molecule details ›
Chains: A, B
Length: 441 amino acids
Theoretical weight: 50.22 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
  • Canonical: O89017 (Residues: 1-435; Coverage: 100%)
Gene names: Lgmn, Prsc1
Sequence domains: Peptidase C13 family
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 51.962Å b: 163.361Å c: 59.278Å
α: 90° β: 104.32° γ: 90°
R R work R free
0.275 0.217 0.275
Expression system: Spodoptera frugiperda