› 2l1w

Solution NMR

The solution structure of soybean calmodulin isoform 4 complexed with the vacuolar calcium ATPase BCA1 peptide

Released:
DOI: 10.2210/pdb2l1w/pdb
PDB entry 2l1w coloured by chain, ensemble of 25 models, front view.
PDB entry 2l1w coloured by chain, ensemble of 25 models, side view.
PDB entry 2l1w coloured by chain, ensemble of 25 models, top view.
Source organism: Glycine max
Primary publication:
The solution structure of a plant calmodulin and the CaM-binding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism.
Ishida H, Vogel HJ
J Biol Chem 285 38502-10 (2010)
PMID: 20880850

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162860 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
EF-hand domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.9 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q39890 (Residues: 2-150; Coverage: 99%)
Gene names: 547787, GLYMA_10G178400, SCaM-4
Sequence domains:
vacuolar calcium ATPase BCA1 peptide Chain: B
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 3.1 KDa
Source organism: Glycine max
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

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

3 mentions without citation

The solution structure of a plant calmodulin and the CaM-binding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism.
Ishida et al. (2010)
2 more