Human prion protein variant V129. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Jan 2010.
Explore 3HAK in 3D Show helices and sheets RCSB PDB PDBe
3HAK contains 6 α-helices and 2 β-strands across 1 chain. 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 | 129-130 | 2 | 1 |
| α-helix | 135-138 | 4 | |
| α-helix | 144-153 | 10 | |
| α-helix | 154-156 | 3 | |
| β-strand | 162-163 | 2 | 1 |
| α-helix | 165-169 | 5 | |
| α-helix | 172-192 | 21 | |
| α-helix | 200-226 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major prion protein | A | protein | 103 | Homo sapiens | P04156 (AlphaFold model) |
>3HAK_1 Major prion protein (chains A) LGGYVLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITI KQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQ
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. Lee, S., Antony, L., Hartmann, R. et al. EMBO J (2010) 29:251-262. DOI 10.1038/emboj.2009.333 · PubMed
Other PDB entries of the same protein (UniProt P04156 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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