4E1H: Fragment of human prion protein

Fragment of human prion protein. Determined by X-ray diffraction at 1.4 Å resolution. Released 6 Mar 2013.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Homo sapiens
Chains: 12
Atoms: 771
Mol. weight: 9.48 kDa
Ligands: CIT, FE
Released: 6 Mar 2013

Explore 4E1H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4E1H contains 0 α-helices and 12 β-strands across 12 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, C and I: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	178-181	4	1

Chains B, D, F, H, J and L: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	212-215	4	1

Chains E, G and K: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	179-181	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Major prion protein	A, C, E, G, I, K	protein	6	Homo sapiens	P04156 (AlphaFold model)
Major prion protein	B, D, F, H, J, L	protein	6	Homo sapiens	P04156 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I, K), FASTA

>4E1H_1 Major prion protein (chains A, C, E, G, I, K)
HDCVNI

Sequence of entity 2 (B, D, F, H, J, L), FASTA

>4E1H_2 Major prion protein (chains B, D, F, H, J, L)
EQMCIT

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	4
FE	FE (III) ion	Fe	3

Primary citation

Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. Apostol, M.I., Perry, K., Surewicz, W.K. J Am Chem Soc (2013) 135:10202-10205. DOI 10.1021/ja403001q · 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
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…
6PQ5 1.5 Å, AGAAAA segment 113-118 from human prion

Browse structure collections

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