Research workbench
Solution structure of MLL4 PHD6 domain in complex with histone H4K16AC peptide
Analyse Solution structure of MLL4 PHD6 domain in complex with histone H4K16AC peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O7G
- Type
- protein
- Length
- 68 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase 2D; Histone H4
- EC
- 2.1.1.43
- UniProt
- O14686
- Ligands
- ZN
Structure
solution nmr · 2 distinct chains · 25% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Histone-lysine N-methyltransferase 2D (EC 2.1.1.43) | protein | 60 | 28% helix, 10% strand | O14686 |
| A | Histone H4 | protein | 8 | 0% helix, 25% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 452 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 6O7G · Solution structure of MLL4 PHD6 domain in complex with histone H4K16ac peptide · the same entry in another collection · chain B against B, 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 O14686
- Elsewhere: RCSB PDB 6O7G · PDBe 6O7G · UniProt O14686
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