PDBe 2r28

X-ray diffraction
1.86Å resolution

The complex Structure of Calmodulin Bound to a Calcineurin Peptide

Released:
Source organism: Homo sapiens
Primary publication:
The complex structure of calmodulin bound to a calcineurin peptide.
Proteins 73 19-27 (2008)
PMID: 18384083

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
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • 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: C, D
Molecule details ›
Chains: C, D
Length: 25 amino acids
Theoretical weight: 2.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q08209 (Residues: 389-413; Coverage: 5%)
Gene names: CALNA, CNA, PPP3CA

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: C2
Unit cell:
a: 120.7Å b: 43.2Å c: 70.9Å
α: 90° β: 109.9° γ: 90°
R-values:
R R work R free
0.23 0.23 0.28
Expression system: Escherichia coli BL21(DE3)