2KJ3: Small s protein

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.

Method
Solid-state NMR
Organism
Podospora anserina
Chains
3
Atoms
1,827
Mol. weight
26 kDa
Released
2 Jun 2010

Explore 2KJ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 5 β-strands

ElementResiduesLengthSheet
α-helix222-2232
β-strand226-23491
β-strand238-24582
β-strand261-270101
β-strand274-28182
β-strand29113
Chain B: 0 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand22314
β-strand225-234101
β-strand238-24582
β-strand25814
β-strand261-270101
β-strand274-28182
β-strand29013
Chain C: 0 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand22315
β-strand225-234101
β-strand238-24582
β-strand25815
β-strand262-27091
β-strand274-28182

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Small s proteinA, B, Cprotein79Podospora anserinaQ03689 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>2KJ3_1 Small s protein (chains A, B, C)
MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVL
IGNEYGGKGFWDNHHHHHH

Primary citation

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:

Browse structure collections

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