Research workbench
AlphaFold monomer V2.0 prediction for pseudouridine-5'-phosphate glycosidase (A5UT22)
Analyse AlphaFold monomer V2.0 prediction for pseudouridine-5'-phosphate glycosidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5UT22
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x41f982d1Ab404B1F39f5162365b91bF104CE6a14
- Molecule
- Pseudouridine-5'-phosphate glycosidase
- UniProt
- A5UT22
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pseudouridine-5'-phosphate glycosidase | protein | 311 | 47% helix, 20% strand | A5UT22 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.68 | 0.81 | 44 | empty |
| 2 | 69 | 0.33 | 0.75 | 11 | empty |
| 3 | 60 | 0.32 | 0.76 | 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 A5UT22
- Elsewhere: UniProt A5UT22 · AlphaFold DB A5UT22
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