A novel conformation of calmodulin. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Mar 2013.
Explore 4HEX in 3D Show helices and sheets RCSB PDB PDBe
4HEX contains 16 α-helices and 8 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 | 10-20 | 11 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 30-39 | 10 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 66-73 | 8 | |
| α-helix | 78-93 | 16 | |
| β-strand | 100-101 | 2 | 2 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 2 |
| α-helix | 139-142 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-20 | 12 | |
| β-strand | 27-28 | 2 | 3 |
| α-helix | 30-39 | 10 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 66-73 | 8 | |
| α-helix | 78-93 | 16 | |
| β-strand | 100-101 | 2 | 4 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 4 |
| α-helix | 139-145 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A, B | protein | 156 | Mus musculus | P0DP26 (AlphaFold model) |
>4HEX_1 Calmodulin (chains A, B) MHHHHHHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI NEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNL GEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
A novel trans conformation of ligand-free calmodulin. Kumar, V., Chichili, V.P.R., Tang, X. et al. PLoS One (2013) 8:e54834-e54834. DOI 10.1371/journal.pone.0054834 · PubMed
Other PDB entries of the same protein (UniProt P0DP26 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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