Research workbench
Crystal structure of dpf domain of moz in complex with H3K14BZ peptide
Analyse Crystal structure of dpf domain of moz in complex with H3K14BZ peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LSB
- Type
- protein
- Length
- 146 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT6A; Histone H3
- EC
- 2.3.1.48
- UniProt
- Q92794
- Ligands
- ZN, NH2
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 121 | 15% helix, 10% strand | Q92794 |
| B | Histone H3 | protein | 25 | 64% helix, 8% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1180 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6LSB · Crystal Structure of DPF domain of MOZ in complex with H3K14bz peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q92794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT6A (Q92794) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q92794
- Elsewhere: RCSB PDB 6LSB · PDBe 6LSB · UniProt Q92794
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