› 3ifk

X-ray diffraction
2.03Å resolution

Crystal Structure Of Calcium-Saturated Calmodulin N-terminal Domain Fragment, Residues 1-90

Released:
DOI: 10.2210/pdb3ifk/pdb
PDB entry 3ifk coloured by chain, front view.
PDB entry 3ifk coloured by chain, side view.
PDB entry 3ifk 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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-144023 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 10.16 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP29 (Residues: 2-91; Coverage: 60%)
Gene names: CaMI, Calm, Calm1, Cam, Cam1
Sequence domains: EF-hand domain pair

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 55.285Å b: 58.851Å c: 67.115Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.293
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Protein Conformational Changes Are Detected and Resolved Site Specifically by Second-Harmonic Generation.
Moree et al. (2015)
6 more

2 mentions without citation

Thermodynamics and conformational change governing domain-domain interactions of calmodulin.
O'Donnell et al. (2009)
1 more