Protein aggregation and alzheimer's disease: crystallographic analysis of the phenomenon. Engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization. Determined by X-ray diffraction at 1.65 Å resolution. Released 8 Sept 2000.
Explore 1CQM in 3D Show helices and sheets RCSB PDB PDBe
1CQM contains 5 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 |
|---|---|---|---|
| β-strand | 2-10 | 9 | 1 |
| α-helix | 16-32 | 17 | |
| β-strand | 36-52 | 17 | 1 |
| β-strand | 55-67 | 13 | 1 |
| α-helix | 69-80 | 12 | |
| β-strand | 85-92 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-10 | 9 | 2 |
| α-helix | 16-32 | 17 | |
| β-strand | 36-52 | 17 | 2 |
| β-strand | 55-67 | 13 | 2 |
| α-helix | 69-71 | 3 | |
| α-helix | 72-80 | 9 | |
| β-strand | 85-92 | 8 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribosomal protein S6 | A, B | protein | 101 | Thermus thermophilus | Q5SLP8 (AlphaFold model) |
>1CQM_1 RIBOSOMAL PROTEIN S6 (chains A, B) MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKVAILGLRRLAYPIAKDPQGYF LWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPFLANA
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. Otzen, D.E., Kristensen, O., Oliveberg, M. Proc Natl Acad Sci U S A (2000) 97:9907-9912. DOI 10.1073/pnas.160086297 · PubMed
Other PDB entries of the same protein (UniProt Q5SLP8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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