Research workbench
Importin-9 bound to H2A-H2B
Analyse Importin-9 bound to H2A-H2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N1Z
- Type
- protein
- Length
- 2,270 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin-9; Histone H2A; Histone H2B 1.1
- UniProt
- Q96P70, Q6AZJ8, P02281
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 6 distinct chains · 73% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin-9 | protein | 961 | 73% helix, 1% strand | Q96P70 |
| B | Histone H2A | protein | 86 | 69% helix, 3% strand | Q6AZJ8 |
| C | Histone H2B 1.1 | protein | 92 | 73% helix, 3% strand | P02281 |
| D | Importin-9 | protein | 949 | 74% helix, 1% strand | Q96P70 |
| E | Histone H2A | protein | 85 | 69% helix, 4% strand | Q6AZJ8 |
| F | Histone H2B 1.1 | protein | 97 | 66% helix, 3% strand | P02281 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.79 | 0.81 | 99 | empty |
| 2 | 602 | 0.78 | 0.84 | 53 | empty |
| 3 | 932 | 0.75 | 0.78 | 74 | empty |
| 4 | 569 | 0.73 | 0.81 | 48 | empty |
| 5 | 519 | 0.69 | 0.79 | 67 | empty |
Interfaces
7 interfaces between chains.
- E–F · 2643 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 2580 Ų buried · 24 hydrogen bonds · protein-protein
- D–F · 2329 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 2050 Ų buried · 24 hydrogen bonds · protein-protein
- D–E · 1004 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 Q96P70
- Every structure of UniProt Q6AZJ8
- Every structure of UniProt P02281
- Elsewhere: RCSB PDB 6N1Z · PDBe 6N1Z · UniProt Q96P70 · UniProt Q6AZJ8 · UniProt P02281
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