Research workbench
Crystal structure of the bromodomain of bromodomain adjacent to zinc finger domain protein 2B (BAZ2B) in complex with 314268-40-1 (SGC - Diamond I04-1 fragment screening)
Analyse Crystal structure of the bromodomain of bromodomain adjacent to zinc finger… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CUB
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Homo sapiens
- Molecule
- Bromodomain adjacent to zinc finger domain protein 2B
- UniProt
- Q9UIF8
- Ligands
- 54V
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · resolution 2.1 · 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 | 115 | 62% helix, 0% strand | Q9UIF8 |
Ligands and binding sites
- 54V · methyl 4-[(4-methylpiperazin-1-yl)methyl]benzoate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 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 | 77 | 0.46 | 0.81 | 20 | 54V |
Compared structures
- 5CUB · Crystal structure of the bromodomain of bromodomain adjacent to zinc finger domain… · 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 0.92
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 5CUB · PDBe 5CUB · UniProt Q9UIF8
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