› 1lkj

Solution NMR

NMR Structure of Apo Calmodulin from Yeast Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb1lkj/pdb
PDB entry 1lkj coloured by chain, ensemble of 31 models, front view.
PDB entry 1lkj coloured by chain, ensemble of 31 models, side view.
PDB entry 1lkj coloured by chain, ensemble of 31 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The solution structure of apocalmodulin from Saccharomyces cerevisiae implies a mechanism for its unique Ca2+ binding property.
Ishida H, Nakashima K, Kumaki Y, Nakata M, Hikichi K, Yazawa M
Biochemistry 41 15536-42 (2002)
PMID: 12501182

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
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: 146 amino acids
Theoretical weight: 16.02 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06787 (Residues: 2-147; Coverage: 99%)
Gene names: CMD1, YBR0904, YBR109C
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

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

9 mentions without citation

Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes.
Haynes et al. (2006)
8 more