Research workbench
Crystal structure of BRD9 in complex with bi-7273
Analyse Crystal structure of BRD9 in complex with bi-7273 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EU1
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BRD9
- UniProt
- Q9H8M2
- Ligands
- 5SW
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BRD9 | protein | 113 | 64% helix, 0% strand | Q9H8M2 |
| B | BRD9 | protein | 113 | 63% helix, 0% strand | Q9H8M2 |
Ligands and binding sites
- 5SW · 4-[4-[(dimethylamino)methyl]-3,5-dimethoxy-phenyl]-2-methyl-2,7-naphthyridin-1-one · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.48 | 0.83 | 18 | 5SW |
| 2 | 71 | 0.46 | 0.82 | 17 | 5SW |
| 3 | 56 | 0.32 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 902 Ų buried · 10 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 Q9H8M2
- Elsewhere: RCSB PDB 5EU1 · PDBe 5EU1 · UniProt Q9H8M2
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