4n6o

X-ray diffraction
1.8Å resolution

Crystal structure of reduced legumain in complex with cystatin E/M

Released:
Source organism: Homo sapiens
Primary publication:
Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.
Angew Chem Int Ed Engl 54 2917-21 (2015)
PMID: 25630877

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-172421 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Legumain Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.64 KDa
Source organism: Homo sapiens
Expression system: Leishmania tarentolae
UniProt:
  • Canonical: Q99538 (Residues: 26-303; Coverage: 67%)
Gene names: LGMN, PRSC1
Sequence domains: Peptidase C13 family
Structure domains: Rossmann fold
Cystatin-M Chain: B
Molecule details ›
Chain: B
Length: 131 amino acids
Theoretical weight: 14.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15828 (Residues: 29-149; Coverage: 100%)
Gene name: CST6
Sequence domains: Cystatin domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 44.58Å b: 85.55Å c: 58.92Å
α: 90° β: 94.61° γ: 90°
R-values:
R R work R free
0.21 0.209 0.231
Expression systems:
  • Leishmania tarentolae
  • Escherichia coli