X-ray diffraction
2.4Å resolution

Catalytic domain of Human Calpain-1


Function and Biology Details

Reaction catalysed:
Broad endopeptidase specificity.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Calpain-1 catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 39.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P07384 (Residues: 29-360; Coverage: 47%)
Gene names: CANPL1, CAPN1, PIG30
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P6122
Unit cell:
a: 90.534Å b: 90.534Å c: 433.102Å
α: 90° β: 90° γ: 120°
R R work R free
0.222 0.22 0.264
Expression system: Escherichia coli BL21(DE3)