GYVLGS segment 127-132 from human prion with V129. Determined by X-ray diffraction at 1.92 Å resolution. Released 4 Aug 2010.
Explore 3NHD in 3D Show helices and sheets RCSB PDB PDBe
3NHD contains 0 α-helices and 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major prion protein | A, B | protein | 6 | Homo sapiens | P04156 (AlphaFold model) |
>3NHD_1 Major prion protein (chains A, B) GYVLGS
Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. Apostol, M.I., Sawaya, M.R., Cascio, D. et al. J Biol Chem (2010) 285:29671-29675. DOI 10.1074/jbc.C110.158303 · 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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