› 4phn

X-ray diffraction
1.79Å resolution

The Structural Basis of Differential Inhibition of Human Calpain by Indole and Phenyl alpha-Mercaptoacrylic Acids

Released:
DOI: 10.2210/pdb4phn/pdb
PDB entry 4phn coloured by chain, front view.
PDB entry 4phn coloured by chain, side view.
PDB entry 4phn coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
The structural basis of differential inhibition of human calpain by indole and phenyl α-mercaptoacrylic acids.
Adams SE, Rizkallah PJ, Miller DJ, Robinson EJ, Hallett MB, Allemann RK
J Struct Biol 187 236-241 (2014)
PMID: 25086406

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calpain small subunit 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 19.88 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P04574 (Residues: 94-266; Coverage: 65%)
Gene names: CAPN4, CAPNS1
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 49.53Å b: 70.56Å c: 58.67Å
α: 90° β: 108.79° γ: 90°
R-values:
R R work R free
0.186 0.183 0.228
Expression system: Escherichia coli

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Citations

2 review citations

An updated patent review of calpain inhibitors (2012 - 2014).
Donkor IO. (2015)
1 more