› 1nx0

X-ray diffraction
2.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-137920 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
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
Calpastatin Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 1.24 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P12675 (Residues: 231-242; Coverage: 2%)
Gene name: CAST
Small molecule inhibitor Chain: E
Molecule details ›
Chain: E
Length: 5 amino acids
Theoretical weight: 474 Da

Ligands and Environments

1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 53.78Å b: 83.3Å c: 92.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.261
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Evolutionary families of peptidase inhibitors.
Rawlings et al. (2004)
9 more

1 mention without citation

Using parallelized incremental meta-docking can solve the conformational sampling issue when docking large ligands to proteins.
Devaurs et al. (2019)