Research workbench
Mouse importin alpha: BIMAX1 peptide complex
Analyse Mouse importin alpha: BIMAX1 peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UKW
- Type
- protein
- Length
- 448 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-2; BIMAX1 peptide
- UniProt
- P52293
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Importin subunit alpha-2 | protein | 426 | 73% helix, 0% strand | P52293 |
| C | BIMAX1 peptide | protein | 22 | 14% helix, 0% strand | — |
Ligands and binding sites
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.49 | 0.84 | 13 | empty |
| 2 | 60 | 0.35 | 0.78 | 8 | BTB |
| 3 | 69 | 0.28 | 0.72 | 21 | empty |
Interfaces
1 interface between chains.
- B–C · 1636 Ų buried · 41 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 3UKW · PDBe 3UKW · UniProt P52293
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