› 2hf5

Solution NMR

The structure and function of a novel two-site calcium-binding fragment of calmodulin

Released:
DOI: 10.2210/pdb2hf5/pdb
PDB 2hf5 coloured by chain and viewed from the front.
PDB 2hf5 coloured by chain and viewed from the side.
PDB 2hf5 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3.
Lakowski TM, Lee GM, Okon M, Reid RE, McIntosh LP
Protein Sci. 16 1119-32 (2007)
PMID: 17473011

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 68 amino acids
Theoretical weight: 7.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 47-114; Coverage: 46%)
Gene names: CALM, CALM1, CAM, CAM1
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: Restrained molecular dynamics, simulated annealing
Expression system: Escherichia coli

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Citations

1 review citation

Ca2+/calmodulin-dependent transcriptional pathways: potential mediators of skeletal muscle growth and development.
Al-Shanti et al. (2009)
15 other articles

2 mentions without citation

Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin.
Tripathi et al. (2009)
1 more