Research workbench
AlphaFold monomer V2.0 prediction for pseudouridine-5'-phosphate glycosidase (A7HMA1)
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
- A7HMA1
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBfaA594FE630D9BE02C43398624E98B6f6c4a20D
- Molecule
- Pseudouridine-5'-phosphate glycosidase
- UniProt
- A7HMA1
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 50% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pseudouridine-5'-phosphate glycosidase | protein | 296 | 50% helix, 20% strand | A7HMA1 |
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 | 183 | 0.69 | 0.88 | 37 | empty |
| 2 | 69 | 0.37 | 0.78 | 12 | empty |
| 3 | 63 | 0.31 | 0.75 | 15 | 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 A7HMA1
- Elsewhere: UniProt A7HMA1 · AlphaFold DB A7HMA1
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