Research workbench
Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3 peptide
Analyse Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QSN
- Type
- protein
- Length
- 173 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TGCN5 histone acetyl transferase; Histone H3
- EC
- 2.3.1.-
- UniProt
- Q27198, P61830
- Ligands
- COA
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TGCN5 histone acetyl transferase (EC 2.3.1.-) | protein | 162 | 36% helix, 30% strand | Q27198 |
| B | Histone H3 | protein | 11 | 0% helix, 0% strand | P61830 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.60 | 0.82 | 23 | COA |
| 2 | 71 | 0.32 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 782 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1QSN · Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain B against A, TM-score 0.29
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 Q27198
- Every structure of UniProt P61830
- Elsewhere: RCSB PDB 1QSN · PDBe 1QSN · UniProt Q27198 · UniProt P61830
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