MolNFT v1 · #117403 · protein
Crystal structure of BAZ2B bromodomain in complex with acetylindole compound UZH47
5E73 · Bromodomain adjacent to zinc finger domain protein 2B: “Crystal structure of BAZ2B bromodomain in complex with acetylindole compound UZH47”. X-ray diffraction, 1 ligand (UO1), 1 pocket (best druggability 0.45). MolNFT v1 #117403 on…
- PDB
- 5E73
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain adjacent to zinc finger domain protein 2B
- UniProt
- Q9UIF8
- Ligands
- UO1
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain adjacent to zinc finger domain protein 2B | protein | 116 | 62% helix, 0% strand | Q9UIF8 |
Ligands and binding sites
- UO1 · N-(1-acetyl-1H-indol-3-yl)-N-(5-hydroxy-2-methylphenyl)acetamide · ligand · chains A
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 | 66 | 0.45 | 0.82 | 16 | UO1 |
Compared structures
- 5E73 · Crystal Structure of BAZ2B bromodomain in complex with acetylindole compound UZH47 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UIF8 · AlphaFold monomer V2.0 prediction for bromodomain adjacent to zinc finger domain protein… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q9UIF8
- Elsewhere: RCSB PDB 5E73 · PDBe 5E73 · UniProt Q9UIF8
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