Research workbench
Crystal structure of AF9 yeats domain in complex with histone H3K9BU
Analyse Crystal structure of AF9 yeats domain in complex with histone H3K9BU in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MIL
- Type
- protein
- Length
- 291 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein af-9; Histone H3K9BU
- UniProt
- P42568
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein af-9 | protein | 138 | 11% helix, 53% strand | P42568 |
| B, D | Histone H3K9BU | protein | 7 | 0% helix, 29% strand | — |
| C | Protein af-9 | protein | 139 | 9% helix, 53% strand | P42568 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 801 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 616 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 565 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
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 P42568
- Elsewhere: RCSB PDB 6MIL · PDBe 6MIL · UniProt P42568
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