› 4fgu

X-ray diffraction
3.9Å resolution

Crystal structure of prolegumain

Released:
DOI: 10.2210/pdb4fgu/pdb
PDB entry 4fgu coloured by chain, front view.
PDB entry 4fgu coloured by chain, side view.
PDB entry 4fgu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
Dall E, Brandstetter H
Proc Natl Acad Sci U S A 110 10940-5 (2013)
PMID: 23776206

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-189215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Legumain Chains: A, B
Molecule details ›
Chains: A, B
Length: 429 amino acids
Theoretical weight: 49.21 KDa
Source organism: Homo sapiens
Expression system: Leishmania tarentolae
UniProt:
  • Canonical: Q99538 (Residues: 18-433; Coverage: 100%)
Gene names: LGMN, PRSC1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: R32
Unit cell:
a: 185.1Å b: 185.1Å c: 173.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.287 0.286 0.3
Expression system: Leishmania tarentolae

Quick links

Citations

19 review citations

Vacuolar processing enzyme in plant programmed cell death.
Hatsugai et al. (2015)
18 more

7 mentions without citation

Asparaginyl endopeptidases: enzymology, applications and limitations.
Tang et al. (2021)
6 more