X-ray diffraction
2.4Å resolution

Crystal Structure of calmodulin complexed with a peptide

Primary publication:
Structural insights into the mechanism of calmodulin binding to death receptors.
Acta Crystallogr. D Biol. Crystallogr. 70 1604-13 (2014)
PMID: 24914971

Function and Biology Details

Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 17.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P0DP23 (Residues: 2-149; Coverage: 99%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Tumor necrosis factor receptor superfamily member 6 Chain: E
Molecule details ›
Chain: E
Length: 25 amino acids
Theoretical weight: 2.7 KDa
Source organism: synthetic construct
Expression system: Not provided
  • Canonical: P25445 (Residues: 230-254; Coverage: 8%)
Gene names: APT1, FAS, FAS1, TNFRSF6

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 40.062Å b: 40.062Å c: 174.431Å
α: 90° β: 90° γ: 120°
R R work R free
0.219 0.217 0.259
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided