MolNFT v2 · #211876 · protein
Crystal structure of importin-alpha1 bound to the HIF-1alpha nuclear localization signal (delta 724-751)
8HE3 · Importin subunit alpha-1: “Crystal structure of importin-alpha1 bound to the HIF-1alpha nuclear localization signal (delta 724-751)”. X-ray diffraction at 1.9, 1 ligand (SO4), 1 pocket (best druggability 0.47). MolNFT v2 #211876 on…
- PDB
- 8HE3
- Type
- protein
- Length
- 430 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Homo sapiens; Mus musculus
- Molecule
- Importin subunit alpha-1; Hypoxia-inducible factor 1-alpha
- UniProt
- P52293
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · resolution 1.9 · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-1 | protein | 422 | 74% helix, 0% strand | P52293 |
| B | Hypoxia-inducible factor 1-alpha | protein | 8 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.47 | 0.82 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 676 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- P52293 · AlphaFold monomer V2.0 prediction for importin subunit alpha-1 (P52293) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 8HE3 · PDBe 8HE3 · UniProt P52293
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