Research workbench
Crystal structure of importin alpha 3 in complex with human LSD1 nls
Analyse Crystal structure of importin alpha 3 in complex with human LSD1 nls in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JJL
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-3; Lysine-specific histone demethylase 1A
- EC
- 1.14.99.66
- UniProt
- O00629, O60341
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-3 | protein | 412 | 73% helix, 0% strand | O00629 |
| B | Lysine-specific histone demethylase 1A (EC 1.14.99.66) | protein | 6 | 0% helix, 0% strand | O60341 |
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 | 58 | 0.38 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 627 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 7JJL · Crystal structure of Importin Alpha 3 in complex with human LSD1 NLS · the same entry in another collection · chain A against A, TM-score 1.00
- O00629 · AlphaFold monomer V2.0 prediction for importin subunit alpha-3 (O00629) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O00629
- Every structure of UniProt O60341
- Elsewhere: RCSB PDB 7JJL · PDBe 7JJL · UniProt O00629 · UniProt O60341
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