3HAK: Human prion protein variant V129

Human prion protein variant V129. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Jan 2010.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
1
Atoms
1,002
Mol. weight
12.37 kDa
Released
12 Jan 2010

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

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand129-13021
α-helix135-1384
α-helix144-15310
α-helix154-1563
β-strand162-16321
α-helix165-1695
α-helix172-19221
α-helix200-22627

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Major prion proteinAprotein103Homo sapiensP04156 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3HAK_1 Major prion protein (chains A)
LGGYVLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITI
KQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQ

Primary citation

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:

Browse structure collections

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