Research workbench
Self-acetylation mediated histone H3 lysine 56 acetylation by RTT109
Analyse Self-acetylation mediated histone H3 lysine 56 acetylation by RTT109 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZFN
- Type
- protein
- Length
- 376 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of TY1 transposition protein 109
- UniProt
- Q07794
- Ligands
- ACO
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of TY1 transposition protein 109 | protein | 376 | 32% helix, 24% strand | Q07794 |
Ligands and binding sites
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 | 326 | 0.73 | 0.85 | 43 | ACO, GOL |
| 2 | 231 | 0.64 | 0.82 | 30 | empty |
| 3 | 145 | 0.46 | 0.77 | 22 | empty |
| 4 | 115 | 0.46 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 7 modified (engineered, acetylation).
Compared structures
- 2ZFN · Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109 · the same entry in another collection · chain A against A, TM-score 1.00
- Q07794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q07794) · 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 Q07794
- Elsewhere: RCSB PDB 2ZFN · PDBe 2ZFN · UniProt Q07794
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