Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (Q7TUG1)
Analyse AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7TUG1
- Type
- protein
- Length
- 517 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb17F0b89Fb447a3F06B40871336A733435186471
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- Q7TUG1
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 517 | 41% helix, 21% strand | Q7TUG1 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 931 | 0.73 | 0.77 | 57 | empty |
| 2 | 226 | 0.50 | 0.75 | 23 | empty |
| 3 | 246 | 0.49 | 0.74 | 23 | empty |
| 4 | 74 | 0.34 | 0.75 | 16 | empty |
| 5 | 67 | 0.30 | 0.74 | 16 | 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 Q7TUG1
- Elsewhere: UniProt Q7TUG1 · AlphaFold DB Q7TUG1
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