3NHD: Major prion protein

GYVLGS segment 127-132 from human prion with V129. Determined by X-ray diffraction at 1.92 Å resolution. Released 4 Aug 2010.

Method
X-ray diffraction
Resolution
1.92 Å
Organism
Homo sapiens
Chains
2
Atoms
94
Mol. weight
1.31 kDa
Released
4 Aug 2010

Explore 3NHD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand2-431
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3-531

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Major prion proteinA, Bprotein6Homo sapiensP04156 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3NHD_1 Major prion protein (chains A, B)
GYVLGS

Primary citation

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:

Browse structure collections

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