Research workbench
Structure of importin beta bound to the ibb domain of importin alpha
Analyse Structure of importin beta bound to the ibb domain of importin alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QGK
- Type
- protein
- Length
- 920 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (importin beta subunit); Protein (importin alpha-2 subunit)
- UniProt
- Q14974, P52292
- Pockets
- 12 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (importin beta subunit) | protein | 876 | 76% helix, 0% strand | Q14974 |
| B | Protein (importin alpha-2 subunit) | protein | 44 | 70% helix, 0% strand | P52292 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.73 | 0.94 | 29 | empty |
| 2 | 165 | 0.69 | 0.88 | 29 | empty |
| 3 | 355 | 0.64 | 0.79 | 38 | empty |
| 4 | 282 | 0.60 | 0.79 | 30 | empty |
| 5 | 211 | 0.49 | 0.75 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 2002 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1QGK · Structure of importin beta bound to the ibb domain of importin alpha · the same entry in another collection · chain A against A, TM-score 1.00
- Q14974 · AlphaFold monomer V2.0 prediction for importin subunit beta-1 (Q14974) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P52292 · AlphaFold monomer V2.0 prediction for importin subunit alpha-1 (P52292) · a predicted model of the same protein · chain B against A, TM-score 0.51
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
- Every structure of UniProt P52292
- Elsewhere: RCSB PDB 1QGK · PDBe 1QGK · UniProt Q14974 · UniProt P52292
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