Research workbench
Cryo-EM structure of amyloid fibril formed by full-length human prion protein
Analyse Cryo-EM structure of amyloid fibril formed by full-length human prion protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LNI
- Type
- protein
- Length
- 600 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- P04156
- Pockets
- 3 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Major prion protein | protein | 60 | 0% helix, 50% strand | P04156 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.77 | 0.86 | 30 | empty |
| 2 | 234 | 0.72 | 0.87 | 34 | empty |
| 3 | 227 | 0.71 | 0.87 | 34 | empty |
Interfaces
17 interfaces between chains.
- H–I · 2691 Ų buried · 75 hydrogen bonds · protein-protein
- C–D · 2685 Ų buried · 75 hydrogen bonds · protein-protein
- B–C · 2675 Ų buried · 71 hydrogen bonds · protein-protein
- I–J · 2675 Ų buried · 70 hydrogen bonds · protein-protein
- G–H · 2674 Ų buried · 72 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 6LNI · Cryo-EM structure of amyloid fibril formed by full-length human prion protein · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04156
- Elsewhere: RCSB PDB 6LNI · PDBe 6LNI · UniProt P04156
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