Research workbench
The double phd finger (dpf) of morf in complex with histone H3K14CR
Analyse The double phd finger (dpf) of morf in complex with histone H3K14CR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OIE
- Type
- protein
- Length
- 254 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT6B; Histone H3.1T peptide
- EC
- 2.3.1.48
- UniProt
- Q8WYB5, Q16695
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histone acetyltransferase KAT6B (EC 2.3.1.48) | protein | 111 | 16% helix, 9% strand | Q8WYB5 |
| C, D | Histone H3.1T peptide | protein | 16 | 50% helix, 13% strand | Q16695 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.66 | 0.96 | 17 | empty |
| 2 | 88 | 0.60 | 0.88 | 21 | empty |
| 3 | 140 | 0.39 | 0.74 | 25 | empty |
| 4 | 62 | 0.38 | 0.80 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–D · 955 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 869 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 435 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6OIE · The double PHD finger (DPF) of MORF in complex with histone H3K14cr · the same entry in another collection · chain A against A, TM-score 1.00
- Q8WYB5 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT6B (Q8WYB5) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q16695 · AlphaFold monomer V2.0 prediction for histone H3.1T (Q16695) · a predicted model of the same protein · chain C against A, TM-score 0.47
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 Q8WYB5
- Every structure of UniProt Q16695
- Elsewhere: RCSB PDB 6OIE · PDBe 6OIE · UniProt Q8WYB5 · UniProt Q16695
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