Research workbench
Structure and assembly of the mouse asc filament by combined NMR spectroscopy and cryo-electron microscopy
Analyse Structure and assembly of the mouse asc filament by combined NMR spectroscopy… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N1F
- Type
- protein
- Length
- 1,335 residues
- Chains
- 15
- Method
- solid-state nmr; electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoptosis-associated speck-like protein
- UniProt
- Q9EPB4
- Pockets
- 10 · best druggability 0.79
Structure
solid-state nmr; electron microscopy · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O | Apoptosis-associated speck-like protein | protein | 89 | 72% helix, 0% strand | Q9EPB4 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 870 | 0.79 | 0.82 | 90 | empty |
| 2 | 1155 | 0.79 | 0.81 | 112 | empty |
| 3 | 1034 | 0.78 | 0.80 | 95 | empty |
| 4 | 656 | 0.73 | 0.80 | 74 | empty |
| 5 | 430 | 0.72 | 0.83 | 54 | empty |
Interfaces
33 interfaces between chains.
- L–M · 455 Ų buried · 7 hydrogen bonds · protein-protein
- I–J · 454 Ų buried · 8 hydrogen bonds · protein-protein
- H–I · 454 Ų buried · 7 hydrogen bonds · protein-protein
- F–G · 453 Ų buried · 8 hydrogen bonds · protein-protein
- G–H · 452 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2N1F · Structure and assembly of the mouse ASC filament by combined NMR spectroscopy and… · the same entry in another collection · chain D against D, 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 Q9EPB4
- Elsewhere: RCSB PDB 2N1F · PDBe 2N1F · UniProt Q9EPB4
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