› 2r9f

X-ray diffraction
1.6Å resolution

Calpain 1 proteolytic core inactivated by ZLAK-3002, an alpha-ketoamide

Released:
DOI: 10.2210/pdb2r9f/pdb
PDB entry 2r9f coloured by chain, front view.
PDB entry 2r9f coloured by chain, side view.
PDB entry 2r9f coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Cocrystal structures of primed side-extending alpha-ketoamide inhibitors reveal novel calpain-inhibitor aromatic interactions.
Qian J, Cuerrier D, Davies PL, Li Z, Powers JC, Campbell RL
J Med Chem 51 5264-70 (2008)
PMID: 18702462

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-161316 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calpain-1 catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 38.8 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P97571 (Residues: 27-356; Coverage: 46%)
Gene names: Capn1, Cls1
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

4 bound ligands:
Ligand CA 2 x CA
Ligand CL 3 x CL
Ligand K2Z 1 x K2Z
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 40.569Å b: 70.568Å c: 110.406Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.222
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

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

5 mentions without citation

Calpain chronicle--an enzyme family under multidisciplinary characterization.
Sorimachi et al. (2011)
4 more