PDBe 1mdw

X-ray diffraction
1.95Å resolution

Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation

Released:
Source organism: Rattus norvegicus
Primary publication:
Calpain silencing by a reversible intrinsic mechanism.
Nat. Struct. Biol. 10 371-8 (2003)
PMID: 12665854

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
Macromolecule:
Calpain-2 catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 36.81 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q07009 (Residues: 19-346; Coverage: 47%)
Gene name: Capn2
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 62.6Å b: 80.6Å c: 75.3Å
α: 90° β: 103.9° γ: 90°
R-values:
R R work R free
0.207 0.207 0.243
Expression system: Escherichia coli BL21(DE3)