Research workbench
Crystal structure of bptf bromo in complex with histone H4K16AC - form II
Analyse Crystal structure of bptf bromo in complex with histone H4K16AC - form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QZT
- Type
- protein
- Length
- 114 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleosome-remodeling factor subunit bptf; Histone H4
- UniProt
- Q12830, P62805
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleosome-remodeling factor subunit bptf | protein | 108 | 66% helix, 0% strand | Q12830 |
| B | Histone H4 | protein | 6 | 0% helix, 0% strand | P62805 |
Ligands and binding sites
- GOL · Glycerol · 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 | 52 | 0.30 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 465 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 3QZT · Crystal Structure of BPTF bromo in complex with histone H4K16ac - Form II · the same entry in another collection · chain A against A, TM-score 1.00
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 Q12830
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 3QZT · PDBe 3QZT · UniProt Q12830 · UniProt P62805
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