Research workbench
Importin Alpha in Complex with the Bipartite NLS of Prp20
Analyse Importin Alpha in Complex with the Bipartite NLS of Prp20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OIH
- Type
- protein
- Length
- 439 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Mus musculus; Saccharomyces cerevisiae
- Molecule
- Importin subunit alpha-1; Guanine nucleotide exchange factor SRM1
- UniProt
- P52293, P21827
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · resolution 2.1 · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-1 | protein | 426 | 73% helix, 0% strand | P52293 |
| B | Guanine nucleotide exchange factor SRM1 | protein | 13 | 0% helix, 0% strand | P21827 |
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 | 75 | 0.46 | 0.82 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1116 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 4OIH · Importin alpha in complex with the bipartite nls of PRP20 · the same entry in another collection · chain A against A, TM-score 1.00
- 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
- P21827 · AlphaFold monomer V2.0 prediction for guanine nucleotide exchange factor SRM1 (P21827) · a predicted model of the same protein · chain B against A, TM-score 0.32
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 P21827
- Elsewhere: RCSB PDB 4OIH · PDBe 4OIH · UniProt P52293 · UniProt P21827
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