Research workbench
Crystal structure of yeast ESA1 hat domain complexed with H4K16COA bisubstrate inhibitor
Analyse Crystal structure of yeast ESA1 hat domain complexed with H4K16COA bisubstrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TO6
- Type
- protein
- Length
- 277 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase ESA1; Histone H4
- EC
- 2.3.1.48
- UniProt
- Q08649, P02309
- Ligands
- CMC
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase ESA1 (EC 2.3.1.48) | protein | 276 | 34% helix, 25% strand | Q08649 |
| B | Histone H4 | protein | 1 | 0% helix, 0% strand | P02309 |
Ligands and binding sites
- CMC · Carboxymethyl coenzyme *A · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 560 | 0.71 | 0.80 | 64 | CMC |
| 2 | 90 | 0.47 | 0.81 | 21 | empty |
| 3 | 64 | 0.33 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 212 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, acetylation).
Compared structures
- 3TO6 · Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q08649 · AlphaFold monomer V2.0 prediction for histone acetyltransferase ESA1 (Q08649) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q08649
- Every structure of UniProt P02309
- Elsewhere: RCSB PDB 3TO6 · PDBe 3TO6 · UniProt Q08649 · UniProt P02309
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