› 1f55

Solution NMR

SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST CALMODULIN

Released:
DOI: 10.2210/pdb1f55/pdb
PDB entry 1f55 coloured by chain, ensemble of 30 models, front view.
PDB entry 1f55 coloured by chain, ensemble of 30 models, side view.
PDB entry 1f55 coloured by chain, ensemble of 30 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Solution structures of the N-terminal domain of yeast calmodulin: Ca2+-dependent conformational change and its functional implication.
Ishida H, Takahashi K, Nakashima K, Kumaki Y, Nakata M, Hikichi K, Yazawa M
Biochemistry 39 13660-8 (2000)
PMID: 11076504

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.55 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P06787 (Residues: 2-78; Coverage: 52%)
Gene names: CMD1, YBR0904, YBR109C
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides.
Yamniuk et al. (2004)
14 other articles

1 mention without citation

Surface dynamics in allosteric regulation of protein-protein interactions: modulation of calmodulin functions by Ca2+.
Kuttner et al. (2013)