Crystal structure of the complex between calmodulin and alphaII-spectrin. Determined by X-ray diffraction at 2.45 Å resolution. Released 5 Sept 2006.
Explore 2FOT in 3D Show helices and sheets RCSB PDB PDBe
2FOT contains 9 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 | 9-19 | 11 | |
| β-strand | 26-27 | 2 | 1 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-53 | 9 | |
| β-strand | 63-64 | 2 | 1 |
| α-helix | 65-71 | 7 | |
| α-helix | 82-92 | 11 | |
| β-strand | 100 | 1 | 2 |
| α-helix | 102-112 | 11 | |
| α-helix | 118-128 | 11 | |
| β-strand | 136 | 1 | 2 |
| α-helix | 138-145 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1191-1210 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 148 | Bos taurus | P62157 (AlphaFold model) |
| alpha-II spectrin Spectrin | C | protein | 42 | Homo sapiens | Q13813 (AlphaFold model) |
>2FOT_1 Calmodulin (chains A) ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEEFVQMMTAK
>2FOT_2 alpha-II spectrin Spectrin (chains C) QQEVYGMMPRDETDSKTASASPWKSARLMVHTVATFNSIKER
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 4 |
Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Simonovic, M., Zhang, Z., Cianci, C.D. et al. J Biol Chem (2006) 281:34333-34340. DOI 10.1074/jbc.M604613200 · 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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