3MD4: Prion peptide
Prion peptide. Determined by X-ray diffraction at 1.15 Å resolution. Released 25 May 2011.
- Method
- X-ray diffraction
- Resolution
- 1.15 Å
- Chains
- 2
- Atoms
- 103
- Mol. weight
- 1.25 kDa
- Released
- 25 May 2011
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Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3MD4 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 | 128-131 | 4 | 1 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Major prion protein | A, B | protein | 6 | | P04156 (AlphaFold model) |
Sequence of entity 1 (A, B), FASTA
>3MD4_1 Major prion protein (chains A, B)
GYMLGS
Primary citation
Diversity in the cross-beta spine structure of prion peptides. Lee, S., Yee, V.C. To be published.
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
- 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…
- 6PQ5 1.5 Å, AGAAAA segment 113-118 from human prion
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