High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR. Determined by solid-state NMR. Released 2 Jun 2010.
Explore 2KJ3 in 3D Show helices and sheets RCSB PDB PDBe
2KJ3 contains 1 α-helix and 18 β-strands across 3 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 | 222-223 | 2 | |
| β-strand | 226-234 | 9 | 1 |
| β-strand | 238-245 | 8 | 2 |
| β-strand | 261-270 | 10 | 1 |
| β-strand | 274-281 | 8 | 2 |
| β-strand | 291 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 223 | 1 | 4 |
| β-strand | 225-234 | 10 | 1 |
| β-strand | 238-245 | 8 | 2 |
| β-strand | 258 | 1 | 4 |
| β-strand | 261-270 | 10 | 1 |
| β-strand | 274-281 | 8 | 2 |
| β-strand | 290 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 223 | 1 | 5 |
| β-strand | 225-234 | 10 | 1 |
| β-strand | 238-245 | 8 | 2 |
| β-strand | 258 | 1 | 5 |
| β-strand | 262-270 | 9 | 1 |
| β-strand | 274-281 | 8 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Small s protein | A, B, C | protein | 79 | Podospora anserina | Q03689 (AlphaFold model) |
>2KJ3_1 Small s protein (chains A, B, C) MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVL IGNEYGGKGFWDNHHHHHH
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy. Van Melckebeke, H., Wasmer, C., Lange, A. et al. J Am Chem Soc (2010) 132:13765-13775. DOI 10.1021/ja104213j · PubMed
Other PDB entries of the same protein (UniProt Q03689 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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