MolNFT v1 · #19728 · protein
Crystal structure of tetrahymena GCN5
1QST · TGCN5 histone acetyl transferase: “Crystal structure of tetrahymena GCN5”. X-ray diffraction, 2 pockets (best druggability 0.53). MolNFT v1 #19728 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QST
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TGCN5 histone acetyl transferase
- UniProt
- Q27198
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TGCN5 histone acetyl transferase | protein | 160 | 35% helix, 29% strand | Q27198 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
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 | 178 | 0.53 | 0.78 | 25 | empty |
| 2 | 135 | 0.47 | 0.78 | 20 | EPE |
Compared structures
- 1QST · Crystal structure of tetrahymena GCN5 · the same entry in another collection · chain A against A, TM-score 1.00
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
- Elsewhere: RCSB PDB 1QST · PDBe 1QST · UniProt Q27198
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