› 2ary

X-ray diffraction
2.4Å resolution

Catalytic domain of Human Calpain-1

Released:
DOI: 10.2210/pdb2ary/pdb
PDB entry 2ary coloured by chain, front view.
PDB entry 2ary coloured by chain, side view.
PDB entry 2ary coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition.
Davis TL, Walker JR, Finerty PJ, Mackenzie F, Newman EM, Dhe-Paganon S
J Mol Biol 366 216-29 (2007)
PMID: 17157313

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • 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:
Ligand CA 4 x CA
Ligand BME 3 x BME
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-values:
R R work R free
0.222 0.22 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Calpain research for drug discovery: challenges and potential.
Ono et al. (2016)
5 more

14 mentions without citation

Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde?
Baudry M. (2019)
13 more