› 2f2o

X-ray diffraction
2.17Å resolution

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

Released:
DOI: 10.2210/pdb2f2o/pdb
PDB entry 2f2o coloured by chain, front view.
PDB entry 2f2o coloured by chain, side view.
PDB entry 2f2o coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode.
Ye Q, Li X, Wong A, Wei Q, Jia Z
Biochemistry 45 738-45 (2006)
PMID: 16411749

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-155735 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin; Protein phosphatase 3 catalytic subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 179 amino acids
Theoretical weight: 19.93 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P62157 (Residues: 1-149; Coverage: 100%)
  • Canonical: P48452 (Residues: 389-413; Coverage: 5%)
Gene names: CALM, CAM, PPP3CA
Sequence domains: EF-hand domain pair
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: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 121.237Å b: 42.769Å c: 71.15Å
α: 90° β: 110.39° γ: 90°
R-values:
R R work R free
0.212 0.204 0.289
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Structural diversity of calmodulin binding to its target sites.
Tidow et al. (2013)
9 more

2 mentions without citation

Methionine oxidation in the calmodulin-binding domain of calcineurin disrupts calmodulin binding and calcineurin activation.
Carruthers et al. (2008)
1 more