Research workbench
Importin-beta-fxfg nucleoporin complex
Analyse Importin-beta-fxfg nucleoporin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F59
- Type
- protein
- Length
- 922 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin beta-1; Fxfg nucleoporin repeats
- UniProt
- Q14974
- Pockets
- 10 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Importin beta-1 | protein | 440 | 73% helix, 0% strand | Q14974 |
| C | Fxfg nucleoporin repeats | protein | 22 | 0% helix, 0% strand | — |
| D | Fxfg nucleoporin repeats | protein | 20 | 0% helix, 0% strand | — |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 281 | 0.59 | 0.78 | 23 | empty |
| 2 | 86 | 0.58 | 0.87 | 20 | empty |
| 3 | 86 | 0.58 | 0.87 | 20 | empty |
| 4 | 238 | 0.56 | 0.78 | 24 | empty |
| 5 | 102 | 0.44 | 0.78 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–C · 904 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 785 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 332 Ų buried · 1 hydrogen bond · 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 Q14974
- Elsewhere: RCSB PDB 1F59 · PDBe 1F59 · UniProt Q14974
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