› 3b32

X-ray diffraction
1.6Å resolution

Crystal Structure of Calcium-Saturated Calmodulin N-Terminal Domain Fragment, Residues 1-75

Released:
DOI: 10.2210/pdb3b32/pdb
PDB entry 3b32 coloured by chain, front view.
PDB entry 3b32 coloured by chain, side view.
PDB entry 3b32 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Thermodynamics and conformational change governing domain-domain interactions of calmodulin.
O'Donnell SE, Newman RA, Witt TJ, Hultman R, Froehlig JR, Christensen AP, Shea MA
Methods Enzymol 466 503-26 (2009)
PMID: 21609874

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-144023 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 8.32 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP29 (Residues: 2-76; Coverage: 50%)
Gene names: CaMI, Calm, Calm1, Cam, Cam1
Sequence domains: EF-hand domain pair

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 34.352Å b: 66.096Å c: 57.823Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.197 0.269
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Effect of Ca2+ on the promiscuous target-protein binding of calmodulin.
Westerlund et al. (2018)
7 more

3 mentions without citation

Basement membrane and stroke.
Yao Y. (2019)
2 more