MolNFT v1 · #148823 · protein
Crystal structure of human BAZ2B phd zinc finger in complex with FR23
6FI1 · Bromodomain adjacent to zinc finger domain protein 2B: “Crystal structure of human BAZ2B phd zinc finger in complex with FR23”. X-ray diffraction, 2 ligands (D3H, ZN), 1 pocket (best druggability 0.48). MolNFT v1 #148823 on…
- PDB
- 6FI1
- Type
- protein
- Length
- 113 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain adjacent to zinc finger domain protein 2B
- UniProt
- Q9UIF8
- Ligands
- D3H, ZN
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain adjacent to zinc finger domain protein 2B | protein | 57 | 18% helix, 14% strand | Q9UIF8 |
| B | Bromodomain adjacent to zinc finger domain protein 2B | protein | 56 | 21% helix, 14% strand | Q9UIF8 |
Ligands and binding sites
- D3H · ~{N}-(4-aminophenyl)-2-azanyl-ethanamide · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A, B
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 | 56 | 0.48 | 0.85 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 802 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6FI1 · Crystal structure of human BAZ2B PHD zinc finger in complex with Fr23 · the same entry in another collection · chain B against B, 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 0.86
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 6FI1 · PDBe 6FI1 · UniProt Q9UIF8
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