Solution structure of the apo N-terminal domain of yeast calmodulin. Determined by solution NMR. Released 15 Jul 2003.
Explore 1F54 in 3D Show helices and sheets RCSB PDB PDBe
1F54 contains 4 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 | 6-18 | 13 | |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 29-39 | 11 | |
| α-helix | 45-53 | 9 | |
| β-strand | 62-64 | 3 | 1 |
| α-helix | 65-72 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 77 | Saccharomyces cerevisiae | P06787 (AlphaFold model) |
>1F54_1 CALMODULIN (chains A) SSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDGN HQIEFSEFLALMSRQLK
Solution Structures of the N-terminal Domain of Yeast Calmodulin: Ca2+-Dependent Conformational Change and Its Functional Implication. Ishida, H., Takahashi, K., Nakashima, K. et al. Biochemistry (2000) 39:13660-13668. DOI 10.1021/bi000582x · PubMed
Other PDB entries of the same protein (UniProt P06787 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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