MolNFT v1 · #45207 · protein
Atomic-resolution 3D structure of amyloid-beta fibrils: the osaka mutation
2MVX · Amyloid beta A4 protein: “Atomic-resolution 3D structure of amyloid-beta fibrils: the osaka mutation”. Solid-state nmr, 4 pockets (best druggability 0.72). MolNFT v1 #45207 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2MVX
- Type
- protein
- Length
- 390 residues
- Chains
- 10
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid beta A4 protein
- UniProt
- P05067
- Pockets
- 4 · best druggability 0.72
Structure
solid-state nmr · 1 distinct chain · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Amyloid beta A4 protein | protein | 39 | 0% helix, 49% 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 | 202 | 0.72 | 0.88 | 42 | empty |
| 2 | 103 | 0.72 | 0.92 | 30 | empty |
| 3 | 107 | 0.70 | 0.91 | 31 | empty |
| 4 | 146 | 0.70 | 0.89 | 40 | empty |
Interfaces
21 interfaces between chains.
- I–J · 1607 Ų buried · 49 hydrogen bonds · protein-protein
- H–I · 1605 Ų buried · 47 hydrogen bonds · protein-protein
- G–H · 1601 Ų buried · 48 hydrogen bonds · protein-protein
- F–G · 1595 Ų buried · 47 hydrogen bonds · protein-protein
- B–C · 1588 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 2MVX · Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation · the same entry in another collection · chain J against J, TM-score 1.00
- P05067 · AlphaFold monomer V2.0 prediction for amyloid-beta precursor protein (P05067) · a predicted model of the same protein · chain E against A, TM-score 0.36
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 2MVX · PDBe 2MVX · UniProt P05067
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