Research workbench
Mouse importin alpha: BIMAX2 peptide complex
Analyse Mouse importin alpha: BIMAX2 peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UKX
- Type
- protein
- Length
- 449 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-2; BIMAX2 peptide
- UniProt
- P52293
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Importin subunit alpha-2 | protein | 426 | 73% helix, 0% strand | P52293 |
| C | BIMAX2 peptide | protein | 23 | 0% helix, 0% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.50 | 0.79 | 23 | empty |
| 2 | 93 | 0.36 | 0.75 | 24 | empty |
Interfaces
1 interface between chains.
- B–C · 1747 Ų buried · 49 hydrogen bonds · 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 P52293
- Elsewhere: RCSB PDB 3UKX · PDBe 3UKX · UniProt P52293
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