Research workbench
Structure of the BRD9 bromodomain and compound 11
Analyse Structure of the BRD9 bromodomain and compound 11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y7H
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 9
- UniProt
- Q9H8M2
- Ligands
- OFK
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bromodomain-containing protein 9 | protein | 114 | 62% helix, 0% strand | Q9H8M2 |
Ligands and binding sites
- OFK · 1-(8-phenylpyrrolo[1,2-a]pyrimidin-6-yl)ethanone · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 430 | 0.60 | 0.75 | 42 | empty |
| 2 | 91 | 0.51 | 0.82 | 16 | OFK |
| 3 | 84 | 0.48 | 0.82 | 16 | OFK |
Interfaces
1 interface between chains.
- A–B · 191 Ų buried · 1 hydrogen bond · 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 6Y7H · PDBe 6Y7H · UniProt Q9H8M2
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