NMR solution structure of apo calmodulin carboxy-terminal domain. Determined by solution NMR. Released 7 Dec 1995.
Explore 1CMF in 3D Show helices and sheets RCSB PDB PDBe
1CMF contains 5 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 82-93 | 12 | |
| β-strand | 100 | 1 | 1 |
| α-helix | 102-108 | 7 | |
| α-helix | 118-122 | 5 | |
| α-helix | 125-127 | 3 | |
| β-strand | 136 | 1 | 1 |
| α-helix | 138-145 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin (vertebrate) | A | protein | 73 | Bos taurus | P62157 (AlphaFold model) |
>1CMF_1 CALMODULIN (VERTEBRATE) (chains A) MKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQ VNYEEFVQMMTAK
Calcium-induced structural changes and domain autonomy in calmodulin. Finn, B.E., Evenas, J., Drakenberg, T. et al. Nat Struct Biol (1995) 2:777-783. DOI 10.1038/nsb0995-777 · PubMed
Other PDB entries of the same protein (UniProt P62157 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1CMF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.