Research workbench
Crystal structure of importin alpha 2 in complex with LSD1 nls S111E mutant
Analyse Crystal structure of importin alpha 2 in complex with LSD1 nls S111E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JK7
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysine-specific histone demethylase 1A; Importin subunit alpha-1
- EC
- 1.14.99.66
- UniProt
- O60341, P52293
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysine-specific histone demethylase 1A (EC 1.14.99.66) | protein | 9 | 0% helix, 0% strand | O60341 |
| B | Importin subunit alpha-1 | protein | 425 | 73% helix, 0% strand | P52293 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains B
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 | 69 | 0.44 | 0.81 | 13 | GOL |
Interfaces
1 interface between chains.
- A–B · 710 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 7JK7 · Crystal structure of Importin alpha 2 in complex with LSD1 NLS S111E mutant · the same entry in another collection · chain A against A, TM-score 1.00
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 O60341
- Every structure of UniProt P52293
- Elsewhere: RCSB PDB 7JK7 · PDBe 7JK7 · UniProt O60341 · UniProt P52293
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