NMR Structure of Apo Calmodulin from Yeast Saccharomyces cerevisiae. Determined by solution NMR. Released 29 Apr 2003.
Explore 1LKJ in 3D Show helices and sheets RCSB PDB PDBe
1LKJ 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 | 6-19 | 14 | |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 29-39 | 11 | |
| α-helix | 45-55 | 11 | |
| β-strand | 62-64 | 3 | 1 |
| α-helix | 65-75 | 11 | |
| α-helix | 81-92 | 12 | |
| β-strand | 99-101 | 3 | 2 |
| α-helix | 102-112 | 11 | |
| α-helix | 118-128 | 11 | |
| β-strand | 134-136 | 3 | 2 |
| α-helix | 137-144 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 146 | Saccharomyces cerevisiae | P06787 (AlphaFold model) |
>1LKJ_1 Calmodulin (chains A) SSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDGN HQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDAE VDDMLREVSDGSGEINIQQFAALLSK
The solution structure of apocalmodulin from Saccharomyces cerevisiae implies a mechanism for its unique Ca2+ binding property. Ishida, H., Nakashima, K., Kumaki, Y. et al. Biochemistry (2002) 41:15536-15542. DOI 10.1021/bi020330r · 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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