MolNFT v1 · #129660 · protein
Near-atomic resolution fibril structure of complete amyloid-BETA(1-42) by cryo-EM
5OQV · Amyloid beta A4 protein: “Near-atomic resolution fibril structure of complete amyloid-BETA(1-42) by cryo-EM”. Electron microscopy, 4 pockets (best druggability 0.69). MolNFT v1 #129660 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5OQV
- Type
- protein
- Length
- 378 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid beta A4 protein
- UniProt
- P05067
- Pockets
- 4 · best druggability 0.69
Structure
electron microscopy · 1 distinct chain · 0% helix, 71% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I | Amyloid beta A4 protein | protein | 42 | 0% helix, 71% strand | P05067 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.69 | 0.90 | 33 | empty |
| 2 | 89 | 0.61 | 0.89 | 26 | empty |
| 3 | 124 | 0.50 | 0.81 | 29 | empty |
| 4 | 92 | 0.50 | 0.83 | 31 | empty |
Interfaces
32 interfaces between chains.
- A–H · 1991 Ų buried · 61 hydrogen bonds · protein-protein
- A–C · 1990 Ų buried · 60 hydrogen bonds · protein-protein
- B–I · 1989 Ų buried · 61 hydrogen bonds · protein-protein
- F–H · 1988 Ų buried · 60 hydrogen bonds · protein-protein
- C–E · 1987 Ų buried · 60 hydrogen bonds · protein-protein
Compared structures
- 5OQV · Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM · the same entry in another collection · chain H against H, TM-score 1.00
- P05067 · AlphaFold monomer V2.0 prediction for amyloid-beta precursor protein (P05067) · a predicted model of the same protein · chain F against A, TM-score 0.28
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 5OQV · PDBe 5OQV · UniProt P05067
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