Research workbench
Crystal structure of TDP2 from C. elegans
Analyse Crystal structure of TDP2 from C. elegans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GEW
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.35
- Source
- Caenorhabditis elegans
- Molecule
- 5'-tyrosyl-DNA phosphodiesterase
- EC
- 3.1.4.-
- UniProt
- Q9XWG3
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · resolution 2.35 · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-tyrosyl-DNA phosphodiesterase (EC 3.1.4.-) | protein | 324 | 30% helix, 27% strand | Q9XWG3 |
Ligands and binding sites
- GOL · Glycerol · additive · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.31 | 0.75 | 16 | GOL |
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 Q9XWG3
- Elsewhere: RCSB PDB 4GEW · PDBe 4GEW · UniProt Q9XWG3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.