PDBe 4nok

X-ray diffraction
2.5Å resolution

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

Released:

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
Macromolecule:
Legumain Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 50.27 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O89017 (Residues: 1-435; Coverage: 100%)
Gene names: Lgmn, Prsc1
Sequence domains: Peptidase C13 family
Structure domains: Topoisomerase I; Chain A, domain 4

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21212
Unit cell:
a: 57.081Å b: 168.908Å c: 49.531Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.202 0.252
Expression system: Spodoptera frugiperda