Research workbench
Crystal structure of human BAZ2B bromodomain in complex with an acetylated histone 3 peptide (H3K14AC)
Analyse Crystal structure of human BAZ2B bromodomain in complex with an acetylated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QC1
- Type
- protein
- Length
- 229 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain adjacent to zinc finger domain protein 2B; Acetylated histone 3 peptide…
- UniProt
- Q9UIF8
- Ligands
- ZN, SO4
Structure
x-ray diffraction · 4 distinct chains · 63% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain adjacent to zinc finger domain protein 2B | protein | 106 | 69% helix, 1% strand | Q9UIF8 |
| B | Bromodomain adjacent to zinc finger domain protein 2B | protein | 106 | 68% helix, 1% strand | Q9UIF8 |
| D | Acetylated histone 3 peptide (H3K14AC) | protein | 8 | 0% helix, 13% strand | — |
| E | Acetylated histone 3 peptide (H3K14AC) | protein | 9 | 0% helix, 11% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–E · 521 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 512 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 337 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (acetylation).
Compared structures
- 4QC1 · Crystal structure of human BAZ2B bromodomain in complex with an acetylated histone 3… · 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 B against A, TM-score 0.97
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 4QC1 · PDBe 4QC1 · UniProt Q9UIF8
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