Research workbench
Importin alpha 3 delta ibb in complex with influenza PB2 nuclear localization domain
Analyse Importin alpha 3 delta ibb in complex with influenza PB2 nuclear localization… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UAE
- Type
- protein
- Length
- 491 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-3; Polymerase basic protein 2
- UniProt
- O00629, P31345
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-3 | protein | 417 | 73% helix, 0% strand | O00629 |
| F | Polymerase basic protein 2 | protein | 74 | 19% helix, 28% strand | P31345 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.50 | 0.76 | 32 | empty |
| 2 | 163 | 0.48 | 0.77 | 23 | empty |
| 3 | 108 | 0.45 | 0.78 | 19 | empty |
| 4 | 105 | 0.41 | 0.77 | 22 | empty |
| 5 | 74 | 0.34 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–F · 1926 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 4UAE · Importin alpha 3 delta IBB in complex with Influenza PB2 Nuclear Localization Domain · the same entry in another collection · chain A against A, TM-score 1.00
- O00629 · AlphaFold monomer V2.0 prediction for importin subunit alpha-3 (O00629) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O00629
- Every structure of UniProt P31345
- Elsewhere: RCSB PDB 4UAE · PDBe 4UAE · UniProt O00629 · UniProt P31345
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