Research workbench
apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis
Analyse apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZJ4
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Thermoproteus uzoniensis
- Molecule
- Trehalose phosphorylase/synthase
- UniProt
- F2L613
- Ligands
- SCN
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| AAA | Trehalose phosphorylase/synthase | protein | 396 | 50% helix, 15% strand | F2L613 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · 2 copies · chains AAA
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 856 | 0.80 | 0.82 | 76 | SCN |
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 F2L613
- Elsewhere: RCSB PDB 6ZJ4 · PDBe 6ZJ4 · UniProt F2L613
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