1CQM: Ribosomal protein S6

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.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Thermus thermophilus
Chains
2
Atoms
1,794
Mol. weight
23.83 kDa
Released
8 Sept 2000

Explore 1CQM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand2-1091
α-helix16-3217
β-strand36-52171
β-strand55-67131
α-helix69-8012
β-strand85-9281
Chain B: 3 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand2-1092
α-helix16-3217
β-strand36-52172
β-strand55-67132
α-helix69-713
α-helix72-809
β-strand85-9282

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribosomal protein S6A, Bprotein101Thermus thermophilusQ5SLP8 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1CQM_1 RIBOSOMAL PROTEIN S6 (chains A, B)
MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKVAILGLRRLAYPIAKDPQGYF
LWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPFLANA

Primary citation

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:

Browse structure collections

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