MolNFT v1 · #80148 · protein
Crystal structure of yeast ESA1 hat domain bound to coenzyme a with active site lysine acetylated
3TO7 · Histone acetyltransferase ESA1: “Crystal structure of yeast ESA1 hat domain bound to coenzyme a with active site lysine acetylated”. X-ray diffraction, 3 ligands (COA, CAD, SO4), 3 pockets (best druggability 0.72). MolNFT v1 #80148…
- PDB
- 3TO7
- 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
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 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 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- CAD · Cacodylic acid · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
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 | 644 | 0.72 | 0.79 | 66 | COA, CAD |
| 2 | 80 | 0.47 | 0.82 | 22 | GOL |
| 3 | 65 | 0.35 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, acetylation).
Compared structures
- 3TO7 · Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine… · 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
- Elsewhere: RCSB PDB 3TO7 · PDBe 3TO7 · UniProt Q08649
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