› 6bdt

X-ray diffraction
2.3Å resolution

Crystal Structure of Human Calpain-3 Protease Core Mutant-C129S

Released:
DOI: 10.2210/pdb6bdt/pdb
PDB entry 6bdt coloured by chain, front view.
PDB entry 6bdt coloured by chain, side view.
PDB entry 6bdt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation.
Ye Q, Campbell RL, Davies PL
J Biol Chem 293 4056-4070 (2018)
PMID: 29382717

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calpain-3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 382 amino acids
Theoretical weight: 44.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20807 (Residues: 46-419; Coverage: 46%)
Gene names: CANP3, CANPL3, CAPN3, NCL1
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand CA 8 x CA
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 59.81Å b: 105.49Å c: 225.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Molecular and cellular basis of genetically inherited skeletal muscle disorders.
Dowling et al. (2021)
4 more

3 mentions without citation

Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation.
Ye et al. (2018)
2 more