Research workbench
AlphaFold monomer V2.0 prediction for nucleoside-triphosphatase THEP1 (Q96YL7)
Analyse AlphaFold monomer V2.0 prediction for nucleoside-triphosphatase THEP1 (Q96YL7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96YL7
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcbd6C743Abc67aE89D40a6eAd06465a8c4D0789f
- Molecule
- Nucleoside-triphosphatase THEP1
- UniProt
- Q96YL7
- Pockets
- 1 · best druggability 0.33
Structure
1 distinct chain · 34% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside-triphosphatase THEP1 | protein | 169 | 34% helix, 32% strand | Q96YL7 |
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 | 100 | 0.33 | 0.73 | 14 | empty |
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 Q96YL7
- Elsewhere: UniProt Q96YL7 · AlphaFold DB Q96YL7
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