3HER: Human prion protein variant F198S with V129

Human prion protein variant F198S with V129. Determined by X-ray diffraction at 1.85 Å resolution. Released 12 Jan 2010.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,794
Mol. weight: 32.38 kDa
Ligands: CD
Released: 12 Jan 2010

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

Secondary structure: helices and β-sheets

3HER contains 14 α-helices and 4 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: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	129-130	2	1
α-helix	131-133	3
α-helix	135-139	5
α-helix	144-153	10
α-helix	154-156	3
β-strand	162-163	2	1
α-helix	164-166	3
α-helix	172-190	19
α-helix	200-222	23

Chain B: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	129-130	2	2
α-helix	131-133	3
α-helix	135-138	4
α-helix	144-153	10
α-helix	154-156	3
β-strand	162-163	2	2
α-helix	164-166	3
α-helix	172-189	18
α-helix	200-226	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Major prion protein	A, B	protein	142	Homo sapiens	P04156 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3HER_1 Major prion protein (chains A, B)
GQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYVLGSAMSRPIIHFGSDYEDRY
YRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENSTETDVKMMERV
VEQMCITQYERESQAYYQRGSS

Ligands and cofactors

ID	Name	Formula	Copies
CD	Cadmium ion	Cd	2

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:

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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