3NHC: Major prion protein

GYMLGS segment 127-132 from human prion with M129. Determined by X-ray diffraction at 1.57 Å resolution. Released 4 Aug 2010.

Method: X-ray diffraction
Resolution: 1.57 Å
Organism: Homo sapiens
Chains: 2
Atoms: 99
Mol. weight: 1.25 kDa
Released: 4 Aug 2010

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

Secondary structure: helices and β-sheets

3NHC 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.

Chains A and B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-5	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Major prion protein	A, B	protein	6	Homo sapiens	P04156 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3NHC_1 Major prion protein (chains A, B)
GYMLGS

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:

2OL9 0.85 Å, Peptide corresponding to residues 170-175 of human prion
7RVE 0.85 Å, Segment from the S170N mutant of the human prion protein 168-176 EYNNQNNFV
7RVJ 1.0 Å, Segment from the human prion protein 169-175 YSNQNNF
7RVK 1.0 Å, Segment from Y169G mutant of the human prion protein 169-175 GSNQNNF
7RVL 1.0 Å, Segment from the Y169F mutant of the human prion protein 168-176 EFSNQNNFV
7RVC 1.0 Å, Segment from the human prion protein 168-176 EYSNQNNFV
3MD4 1.15 Å, Prion peptide
3MD5 1.4 Å, Prion peptide
4E1H 1.4 Å, Fragment of human prion protein
6PQA 1.46 Å, GAVVGG segment 119-124 from human prion
4KML 1.5 Å, Probing the N-terminal beta-sheet conversion in the crystal structure of the full-length…
4N9O 1.5 Å, Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion…

Browse structure collections

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