Research workbench
High-resolution structure of the het-S(218-289) prion in its amyloid form obtained by solid-state NMR
Analyse High-resolution structure of the het-S(218-289) prion in its amyloid form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KJ3
- Type
- protein
- Length
- 237 residues
- Chains
- 3
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q03689
Structure
solid-state nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 79 | — | Q03689 |
Compared structures
- 2KJ3 · High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03689 · AlphaFold monomer V2.0 prediction for heterokaryon incompatibility protein S (Q03689) · a predicted model of the same protein · chain A against A, TM-score 0.68
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q03689
- Elsewhere: RCSB PDB 2KJ3 · PDBe 2KJ3 · UniProt Q03689
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