X-ray diffraction
1.45Å resolution

High-resolution structure of the complex between calmodulin and a peptide from calcineurin A


Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-2 Chains: A, B, E, F
Molecule details ›
Chains: A, B, E, F
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P0DP24 (Residues: 1-149; Coverage: 100%)
Gene names: CALM2, CAM2, CAMB
Sequence domains: EF-hand domain pair
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Chains: K, L, M, O
Molecule details ›
Chains: K, L, M, O
Length: 17 amino acids
Theoretical weight: 1.96 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q08209 (Residues: 395-411; Coverage: 3%)
Gene names: CALNA, CNA, PPP3CA

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21
Unit cell:
a: 65.31Å b: 81.32Å c: 71.19Å
α: 90° β: 111.28° γ: 90°
R R work R free
0.187 0.186 0.217
Expression systems:
  • Escherichia coli
  • Not provided