Research workbench
AlphaFold monomer V2.0 prediction for BIS(5'-nucleosyl)-tetraphosphatase prpe [asymmetrical] (Q65LA0)
Analyse AlphaFold monomer V2.0 prediction for BIS(5'-nucleosyl)-tetraphosphatase prpe… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q65LA0
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcbd6C743Abc67aE89D40a6eAd06465a8c4D0789f
- Molecule
- BIS(5'-nucleosyl)-tetraphosphatase prpe [asymmetrical]
- UniProt
- Q65LA0
- Pockets
- 2 · best druggability 0.63
Structure
1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BIS(5'-nucleosyl)-tetraphosphatase prpe [asymmetrical] | protein | 246 | 34% helix, 22% strand | Q65LA0 |
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 | 125 | 0.63 | 0.87 | 21 | empty |
| 2 | 276 | 0.60 | 0.79 | 29 | 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 Q65LA0
- Elsewhere: UniProt Q65LA0 · AlphaFold DB Q65LA0
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