3HEQ: Human prion protein variant D178N with M129

Human prion protein variant D178N with M129. 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: 2
Atoms: 1,947
Mol. weight: 32.56 kDa
Ligands: CD
Released: 12 Jan 2010

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

Secondary structure: helices and β-sheets

3HEQ contains 13 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	135-138	4
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	200-227	28

Chain B: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	129-130	2	2
α-helix	131-133	3
α-helix	135-137	3
α-helix	144-153	10
α-helix	154-156	3
β-strand	162-163	2	2
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

>3HEQ_1 Major prion protein (chains A, B)
GQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRY
YRENMHRYPNQVYYRPMDEYSNQNNFVHNCVNITIKQHTVTTTTKGENFTETDVKMMERV
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

About this viewer

MolViewer shows 3HEQ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.