X-ray diffraction
2.8Å resolution

Crystal Structure of Human Calpain-3 Protease Core in Complex with E-64


Function and Biology Details

Reaction catalysed:
Broad endopeptidase activity
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Calpain-3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 382 amino acids
Theoretical weight: 44.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P20807 (Residues: 46-419; Coverage: 46%)
Gene names: CANP3, CANPL3, CAPN3, NCL1
Sequence domains: Calpain family cysteine protease

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 60.28Å b: 105.36Å c: 225.36Å
α: 90° β: 90° γ: 90°
R R work R free
0.208 0.206 0.264
Expression system: Escherichia coli BL21(DE3)