Research workbench
Type I beta-amyloid 42 filaments from human brain
Analyse Type I beta-amyloid 42 filaments from human brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q4B
- Type
- protein
- Length
- 340 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid-beta precursor protein
- UniProt
- P05067
- Ligands
- UNX
- Pockets
- 2 · best druggability 0.65
Structure
electron microscopy · 1 distinct chain · 0% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R, A, B, C, D, E, F, G, H, I | Amyloid-beta precursor protein | protein | 34 | 0% helix, 56% strand | P05067 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 10 copies · chains R, D, A, E, B, C, F, G, H, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.65 | 0.90 | 32 | empty |
| 2 | 107 | 0.55 | 0.84 | 31 | empty |
Interfaces
31 interfaces between chains.
- B–F · 1345 Ų buried · 38 hydrogen bonds · protein-protein
- R–B · 1341 Ų buried · 36 hydrogen bonds · protein-protein
- C–G · 1339 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 1333 Ų buried · 35 hydrogen bonds · protein-protein
- R–D · 1333 Ų buried · 35 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 P05067
- Elsewhere: RCSB PDB 7Q4B · PDBe 7Q4B · UniProt P05067
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