MolNFT v1 · #183741 · protein
Amyloid beta oligomer displayed on the alpha hemolysin scaffold
7O1Q · Alpha-hemolysin hybridized abeta: “Amyloid beta oligomer displayed on the alpha hemolysin scaffold”. Electron microscopy, 20 pockets (best druggability 0.82). MolNFT v1 #183741 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 7O1Q
- Type
- protein
- Length
- 2,051 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-hemolysin hybridized abeta
- UniProt
- P09616, P05067
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 2% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Alpha-hemolysin hybridized abeta | protein | 293 | 2% helix, 59% strand | P09616, P05067 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 715 | 0.82 | 0.86 | 90 | empty |
| 2 | 501 | 0.82 | 0.88 | 78 | empty |
| 3 | 707 | 0.75 | 0.81 | 76 | empty |
| 4 | 286 | 0.74 | 0.87 | 52 | empty |
| 5 | 184 | 0.73 | 0.89 | 34 | empty |
Interfaces
14 interfaces between chains.
- F–G · 2734 Ų buried · 54 hydrogen bonds · protein-protein
- E–F · 2733 Ų buried · 54 hydrogen bonds · protein-protein
- B–C · 2732 Ų buried · 54 hydrogen bonds · protein-protein
- C–D · 2730 Ų buried · 54 hydrogen bonds · protein-protein
- D–E · 2730 Ų buried · 54 hydrogen bonds · protein-protein
Compared structures
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 P09616
- Every structure of UniProt P05067
- Elsewhere: RCSB PDB 7O1Q · PDBe 7O1Q · UniProt P09616 · UniProt P05067
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