Research workbench
TPX2:IMPORTIN-alpha complex
Analyse TPX2:IMPORTIN-alpha complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KND
- Type
- protein
- Length
- 444 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-2; Targeting protein for XKLP2
- UniProt
- P52293, Q9I8N0
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-2 | protein | 428 | 73% helix, 0% strand | P52293 |
| B | Targeting protein for XKLP2 | protein | 16 | 0% helix, 0% strand | Q9I8N0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.45 | 0.82 | 12 | empty |
| 2 | 64 | 0.33 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1271 Ų buried · 31 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
- Every structure of UniProt Q9I8N0
- Elsewhere: RCSB PDB 3KND · PDBe 3KND · UniProt P52293 · UniProt Q9I8N0
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