› 2nqa

X-ray diffraction
2.2Å resolution

Catalytic Domain of Human Calpain 8

Released:
DOI: 10.2210/pdb2nqa/pdb
PDB entry 2nqa coloured by chain, front view.
PDB entry 2nqa coloured by chain, side view.
PDB entry 2nqa coloured by chain, top view.
Source organisms:
Entry authors: Davis TL, Paramanathan R, Butler-Cole C, Finerty Jr PJ, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-107995 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calpain-2 catalytic subunit; Calpain-8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 36.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P17655 (Residues: 24-346; Coverage: 46%)
  • Canonical: A6NHC0 (Residues: 23-346; Coverage: 46%)
Gene names: CANPL2, CAPN2, CAPN8, NCL2
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases
Leupeptin Inhibitor Chains: D, E
Molecule details ›
Chains: D, E
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Streptomyces roseus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 5 x CA
1 modified residue:
Ligand CSO 10 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P61
Unit cell:
a: 91.794Å b: 91.794Å c: 194.592Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.268
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

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