› 1tlo

X-ray diffraction
1.9Å resolution

High resolution crystal structure of calpain I protease core in complex with E64

Released:
DOI: 10.2210/pdb1tlo/pdb
PDB entry 1tlo coloured by chain, front view.
PDB entry 1tlo coloured by chain, side view.
PDB entry 1tlo coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site.
Moldoveanu T, Campbell RL, Cuerrier D, Davies PL
J Mol Biol 343 1313-26 (2004)
PMID: 15491615

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(DE3)
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 E64 1 x E64
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 40.52Å b: 69.76Å c: 108.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.272 0.238 0.272
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Cysteine cathepsin proteases as pharmacological targets in cancer.
Palermo et al. (2008)
11 more

4 mentions without citation

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