MolNFT v1 · #76475 · protein
Crystal structure of RTT109-ac-CoA complex
3QM0 · Histone acetyltransferase RTT109: “Crystal structure of RTT109-ac-CoA complex”. X-ray diffraction, 2 ligands (ACO, HG), 5 pockets (best druggability 0.74). MolNFT v1 #76475 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3QM0
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase RTT109
- EC
- 2.3.1.48
- UniProt
- Q07794
- Ligands
- ACO, HG
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase RTT109 (EC 2.3.1.48) | protein | 355 | 30% helix, 24% strand | Q07794 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 358 | 0.74 | 0.85 | 40 | HG, ACO |
| 2 | 246 | 0.60 | 0.80 | 30 | empty |
| 3 | 89 | 0.41 | 0.78 | 12 | empty |
| 4 | 87 | 0.40 | 0.77 | 17 | HG |
| 5 | 91 | 0.35 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
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 Q07794
- Elsewhere: RCSB PDB 3QM0 · PDBe 3QM0 · UniProt Q07794
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.