Research workbench
Crystal structure of acetyltransferase from thermus thermophilus HB8
Analyse Crystal structure of acetyltransferase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EXN
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable acetyltransferase
- UniProt
- Q5SLW7
- Ligands
- ACO, CL
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable acetyltransferase | protein | 154 | 34% helix, 32% strand | Q5SLW7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.67 | 0.84 | 29 | ACO |
| 2 | 209 | 0.51 | 0.76 | 20 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3EXN · Crystal structure of acetyltransferase from Thermus thermophilus HB8 · 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 Q5SLW7
- Elsewhere: RCSB PDB 3EXN · PDBe 3EXN · UniProt Q5SLW7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.