The 1.8 angstrom structure of calmodulin rs20 peptide complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 24 Jun 2003.
Explore 1QS7 in 3D Show helices and sheets RCSB PDB PDBe
1QS7 contains 19 α-helices and 8 β-strands across 4 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 | 6-19 | 14 | |
| β-strand | 26-27 | 2 | 1 |
| α-helix | 29-39 | 11 | |
| α-helix | 45-55 | 11 | |
| β-strand | 63-64 | 2 | 1 |
| α-helix | 65-73 | 9 | |
| α-helix | 74-77 | 4 | |
| α-helix | 78-92 | 15 | |
| β-strand | 100 | 1 | 2 |
| α-helix | 102-112 | 11 | |
| α-helix | 118-128 | 11 | |
| β-strand | 136 | 1 | 2 |
| α-helix | 138-146 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-18 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-19 | 14 | |
| β-strand | 26-27 | 2 | 3 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-55 | 11 | |
| β-strand | 63-64 | 2 | 3 |
| α-helix | 65-73 | 9 | |
| α-helix | 78-92 | 15 | |
| β-strand | 99-100 | 2 | 4 |
| α-helix | 102-112 | 11 | |
| α-helix | 118-128 | 11 | |
| β-strand | 136-137 | 2 | 4 |
| α-helix | 138-145 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-18 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A, C | protein | 145 | Escherichia coli | A0MMD0 (AlphaFold model) |
| RS20 | B, D | protein | 21 | P11799 (AlphaFold model) |
>1QS7_1 CALMODULIN (chains A, C) LTDEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTI DFPEFLNLMARKMKDTDSEEELKEAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDE MIREADVDGDGQVNYEEFVQVMMAK
>1QS7_2 RS20 (chains B, D) RRKWQKTGHAVRAIGRLSSSX
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 8 |
High Resolution Structure of a Calmodulin Rs20 Peptide Complex. Weigand, S., Shuvalova, L., Lukas, T.J. et al. To be published.
Other PDB entries of the same protein (UniProt A0MMD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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