Research workbench
Crystal structure of closed dimer of human importin-ALPHA1 (RCH1)
Analyse Crystal structure of closed dimer of human importin-ALPHA1 (RCH1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WPT
- Type
- protein
- Length
- 845 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-1
- UniProt
- P52292
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-1 | protein | 422 | 72% helix, 0% strand | P52292 |
| B | Importin subunit alpha-1 | protein | 423 | 72% helix, 0% strand | P52292 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 17 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 887 | 0.79 | 0.81 | 77 | PEG |
| 2 | 729 | 0.75 | 0.81 | 76 | PEG |
| 3 | 120 | 0.55 | 0.83 | 20 | empty |
| 4 | 107 | 0.53 | 0.83 | 20 | empty |
| 5 | 68 | 0.49 | 0.84 | 13 | PEG |
Interfaces
1 interface between chains.
- A–B · 2091 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 3WPT · Crystal structure of closed dimer of human importin-alpha1 (Rch1) · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.97
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 P52292
- Elsewhere: RCSB PDB 3WPT · PDBe 3WPT · UniProt P52292
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.