› 2nqi

X-ray diffraction
2.04Å resolution

Calpain 1 proteolytic core inactivated by WR13(R,R), an epoxysuccinyl-type inhibitor.

Released:
DOI: 10.2210/pdb2nqi/pdb
PDB entry 2nqi coloured by chain, front view.
PDB entry 2nqi coloured by chain, side view.
PDB entry 2nqi coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Development of calpain-specific inactivators by screening of positional scanning epoxide libraries.
Cuerrier D, Moldoveanu T, Campbell RL, Kelly J, Yoruk B, Verhelst SHL, Greenbaum D, Bogyo M, Davies PL
J Biol Chem 282 9600-9611 (2007)
PMID: 17218315

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: 26-356; Coverage: 46%)
Gene names: Capn1, Cls1
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand NQI 1 x NQI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 40.369Å b: 70.06Å c: 110.743Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

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

1 mention without citation

Design, synthesis, and optimization of novel epoxide incorporating peptidomimetics as selective calpain inhibitors.
Schiefer et al. (2013)