Research workbench
AlphaFold monomer V2.0 prediction for nucleoside-triphosphatase THEP1 (Q97AR1)
Analyse AlphaFold monomer V2.0 prediction for nucleoside-triphosphatase THEP1 (Q97AR1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q97AR1
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Nucleoside-triphosphatase THEP1
- UniProt
- Q97AR1
- Pockets
- 1 · best druggability 0.40
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside-triphosphatase THEP1 | protein | 178 | 35% helix, 30% strand | Q97AR1 |
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 | 53 | 0.40 | 0.82 | 19 | 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 Q97AR1
- Elsewhere: UniProt Q97AR1 · AlphaFold DB Q97AR1
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