MolNFT v1 · #80150 · protein
Crystal structure of yeast ESA1 E338Q hat domain bound to coenzyme a with active site lysine acetylated
3TO9 · Histone acetyltransferase ESA1: “Crystal structure of yeast ESA1 E338Q hat domain bound to coenzyme a with active site lysine acetylated”. X-ray diffraction, 3 ligands (COA, CAD, SO4), 4 pockets (best druggability 0.68). MolNFT v1…
- PDB
- 3TO9
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase ESA1
- EC
- 2.3.1.48
- UniProt
- Q08649
- Ligands
- COA, CAD, SO4
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase ESA1 (EC 2.3.1.48) | protein | 276 | 33% helix, 25% strand | Q08649 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- CAD · Cacodylic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
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 | 411 | 0.68 | 0.80 | 49 | COA, CAD |
| 2 | 187 | 0.54 | 0.79 | 21 | empty |
| 3 | 88 | 0.46 | 0.81 | 21 | empty |
| 4 | 74 | 0.38 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 3TO9 · Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site… · 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 0.94
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
- Elsewhere: RCSB PDB 3TO9 · PDBe 3TO9 · UniProt Q08649
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