Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (Q7VDS0)
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
- Q7VDS0
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC7DFEA189D67fDEA5e8f3ACCc9C756390e523774
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- Q7VDS0
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 518 | 40% helix, 20% strand | Q7VDS0 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1061 | 0.78 | 0.80 | 83 | empty |
| 2 | 226 | 0.55 | 0.78 | 25 | empty |
| 3 | 87 | 0.36 | 0.76 | 16 | empty |
| 4 | 58 | 0.28 | 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 Q7VDS0
- Elsewhere: UniProt Q7VDS0 · AlphaFold DB Q7VDS0
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