Research workbench
Mixing ABETA(1-40) and ABETA(1-42) peptides generates unique amyloid fibrils
Analyse Mixing ABETA(1-40) and ABETA(1-42) peptides generates unique amyloid fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TI6
- Type
- protein
- Length
- 496 residues
- Chains
- 16
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid-beta precursor protein
- UniProt
- P05067
- Pockets
- 4 · best druggability 0.81
Structure
solid-state nmr · 2 distinct chains · 0% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | Amyloid-beta precursor protein | protein | 30 | 0% helix, 43% strand | P05067 |
| B, D, F, H, J, L, N, P | Amyloid-beta precursor protein | protein | 32 | 0% helix, 53% strand | P05067 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.81 | 0.91 | 76 | empty |
| 2 | 383 | 0.81 | 0.90 | 75 | empty |
| 3 | 735 | 0.71 | 0.78 | 72 | empty |
| 4 | 623 | 0.67 | 0.77 | 68 | empty |
Interfaces
44 interfaces between chains.
- K–L · 1273 Ų buried · 40 hydrogen bonds · protein-protein
- J–K · 1270 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 1269 Ų buried · 38 hydrogen bonds · protein-protein
- M–N · 1268 Ų buried · 37 hydrogen bonds · protein-protein
- E–F · 1267 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 6TI6 · Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils · the same entry in another collection · chain K against K, 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 P05067
- Elsewhere: RCSB PDB 6TI6 · PDBe 6TI6 · UniProt P05067
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