Research workbench
Mouse TRIM66 phd-bromo dual domain complexed with the H3(1-24) K9ME3K18AC peptide
Analyse Mouse TRIM66 phd-bromo dual domain complexed with the H3(1-24) K9ME3K18AC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EBK
- Type
- protein
- Length
- 192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tripartite motif-containing protein 66; H3K9ME3K18AC
- UniProt
- E9PZP2
- Ligands
- ALY, ZN
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripartite motif-containing protein 66 | protein | 183 | 42% helix, 4% strand | E9PZP2 |
| B | H3K9ME3K18AC | protein | 9 | 0% helix, 44% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.46 | 0.84 | 16 | ALY |
| 2 | 83 | 0.44 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 649 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 7EBK · Mouse Trim66 PHD-Bromo dual domain complexed with the H3(1-24)K9me3K18ac 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 E9PZP2
- Elsewhere: RCSB PDB 7EBK · PDBe 7EBK · UniProt E9PZP2
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