MolNFT v1 · #89963 · protein
The crystal structure of the dimeric human importin alpha 1 at 2.5 ångström resolution.
4E4V · Importin subunit alpha-2: “The crystal structure of the dimeric human importin alpha 1 at 2.5 ångström resolution.”. X-ray diffraction, 8 pockets (best druggability 0.76). MolNFT v1 #89963 on GenesisL1: 3D structure, binding sites…
- PDB
- 4E4V
- Type
- protein
- Length
- 866 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-2
- UniProt
- P52292
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Importin subunit alpha-2 | protein | 433 | 72% helix, 0% strand | P52292 |
Ligands and binding sites
- GOL · Glycerol · additive · 13 copies · chains A, B
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 2 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.76 | 0.79 | 93 | GOL |
| 2 | 756 | 0.72 | 0.78 | 57 | GOL |
| 3 | 240 | 0.61 | 0.81 | 38 | GOL |
| 4 | 118 | 0.56 | 0.84 | 26 | empty |
| 5 | 82 | 0.51 | 0.84 | 13 | DTT |
Interfaces
1 interface between chains.
- A–B · 2771 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
- 4E4V · The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution. · 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 A against A, TM-score 0.95
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 4E4V · PDBe 4E4V · UniProt P52292
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