Calmodulin, NMR, 30 structures. Determined by solution NMR. Released 1 Aug 1996.
Explore 1DMO in 3D Show helices and sheets RCSB PDB PDBe
1DMO contains 8 α-helices and 4 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 | 6-18 | 13 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 29-39 | 11 | |
| α-helix | 45-55 | 11 | |
| β-strand | 62-63 | 2 | 1 |
| α-helix | 65-76 | 12 | |
| α-helix | 82-90 | 9 | |
| β-strand | 100-101 | 2 | 2 |
| α-helix | 102-112 | 11 | |
| α-helix | 118-125 | 8 | |
| β-strand | 135-136 | 2 | 2 |
| α-helix | 138-143 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 148 | Xenopus laevis | P0DP33 (AlphaFold model) |
>1DMO_1 CALMODULIN (chains A) ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE VDEMIREANIDGDGQVNYEEFVQMMTAK
Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Zhang, M., Tanaka, T., Ikura, M. Nat Struct Biol (1995) 2:758-767. DOI 10.1038/nsb0995-758 · PubMed
Other PDB entries of the same protein (UniProt P0DP33 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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