Research workbench
Crystal structure of bptf phd-linker-bromo in complex with histone H4K12AC peptide
Analyse Crystal structure of bptf phd-linker-bromo in complex with histone H4K12AC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QZV
- Type
- protein
- Length
- 173 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
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleosome-remodeling factor subunit bptf | protein | 167 | 49% helix, 7% strand | Q12830 |
| C | Histone H4 | protein | 6 | 0% helix, 0% strand | P62805 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 451 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 3QZV · Crystal Structure of BPTF PHD-linker-bromo in complex with histone H4K12ac peptide · 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 3QZV · PDBe 3QZV · UniProt Q12830 · UniProt P62805
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