Motions of calmodulin-single-conformer refinement. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Mar 1998.
Explore 1CM1 in 3D Show helices and sheets RCSB PDB PDBe
1CM1 contains 10 α-helices and 4 β-strands across 2 chains. 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 | 6-19 | 14 | |
| β-strand | 27 | 1 | 1 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-55 | 11 | |
| β-strand | 63 | 1 | 1 |
| α-helix | 65-73 | 9 | |
| α-helix | 75-78 | 4 | |
| α-helix | 84-92 | 9 | |
| β-strand | 99-100 | 2 | 2 |
| α-helix | 102-111 | 10 | |
| α-helix | 118-128 | 11 | |
| β-strand | 136-137 | 2 | 2 |
| α-helix | 138-145 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 295-309 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 148 | Bos taurus | P62157 (AlphaFold model) |
| Calmodulin-dependent protein kinase II-alpha | B | protein | 25 | Bos taurus | P11275 (AlphaFold model) |
>1CM1_1 CALMODULIN (chains A) ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEEFVQMMTAK
>1CM1_2 CALMODULIN-DEPENDENT PROTEIN KINASE II-ALPHA (chains B) LKKFNARRKLKGAILTTMLATRNFS
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 5 |
Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering. Wall, M.E., Clarage, J.B., Phillips Jr., G.N. Structure (1997) 5:1599-1612. DOI 10.1016/S0969-2126(97)00308-0 · PubMed
Other PDB entries of the same protein (UniProt P62157 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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