Research workbench
42-residue beta amyloid fibril
Analyse 42-residue beta amyloid fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MXU
- Type
- protein
- Length
- 384 residues
- Chains
- 12
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid beta A4 protein
- UniProt
- P05067
- Pockets
- 3 · best druggability 0.74
Structure
solid-state nmr · 1 distinct chain · 0% helix, 69% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Amyloid beta A4 protein | protein | 32 | 0% helix, 69% strand | P05067 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.74 | 0.76 | 76 | empty |
| 2 | 58 | 0.62 | 0.91 | 24 | empty |
| 3 | 97 | 0.32 | 0.72 | 34 | empty |
Interfaces
13 interfaces between chains.
- K–L · 1363 Ų buried · 34 hydrogen bonds · protein-protein
- J–K · 1354 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 1353 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 1341 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 1335 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 2MXU · 42-Residue Beta Amyloid Fibril · the same entry in another collection · chain L against L, 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 2MXU · PDBe 2MXU · UniProt P05067
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