Research workbench
AlphaFold monomer V2.0 prediction for pseudouridine-5'-phosphate glycosidase (B1HV79)
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
- B1HV79
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Pseudouridine-5'-phosphate glycosidase
- UniProt
- B1HV79
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pseudouridine-5'-phosphate glycosidase | protein | 304 | 49% helix, 18% strand | B1HV79 |
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 | 211 | 0.70 | 0.87 | 35 | empty |
| 2 | 57 | 0.41 | 0.81 | 13 | empty |
| 3 | 78 | 0.36 | 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 B1HV79
- Elsewhere: UniProt B1HV79 · AlphaFold DB B1HV79
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