1I4M: Major prion protein

Crystal structure of the human prion protein reveals a mechanism for oligomerization. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Feb 2002.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,005
Mol. weight
12.98 kDa
Ligands
CD
Released
27 Feb 2002

Explore 1I4M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I4M contains 8 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: 8 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand129-13021
α-helix131-1333
α-helix135-1384
α-helix144-15310
α-helix154-1563
β-strand162-16321
α-helix166-1683
α-helix172-18918
α-helix194-1974
α-helix200-22324

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Major prion proteinAprotein108Homo sapiensP04156 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1I4M_1 MAJOR PRION PROTEIN (chains A)
GAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHD
CVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYY

Ligands and cofactors

IDNameFormulaCopies
CDCadmium ionCd2

Water and common crystallization additives (CL) are not listed.

Primary citation

Crystal structure of the human prion protein reveals a mechanism for oligomerization. Knaus, K.J., Morillas, M., Swietnicki, W. et al. Nat Struct Biol (2001) 8:770-774. DOI 10.1038/nsb0901-770 · 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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