MolNFT v1 · #158883 · protein
Solution structure of MLL4 PHD6 domain in complex with histone H4K16AC peptide
6O7G · Histone-lysine N-methyltransferase 2D: “Solution structure of MLL4 PHD6 domain in complex with histone H4K16AC peptide”. Solution nmr, 1 ligand (ZN). MolNFT v1 #158883 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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